Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions.


Abstract

To evaluate the contribution of the amino acid residues on the surface of a protein to its stability, a series of hydrophobic mutant human lysozymes (Val to Gly, Ala, Leu, Ile, Met, and Phe) modified at three different positions on the surface, which are located in the alpha-helix (Val 110), the beta-sheet (Val 2), and the loop (Val 74), were constructed. Their thermodynamic parameters of denaturation and crystal structures were examined by calorimetry and by X-ray crystallography at 100 K, respectively. Differences in the denaturation Gibbs energy change between the wild-type and the hydrophobic mutant proteins ranged from 4.6 to -9.6 kJ/mol, 2.7 to -1.5 kJ/mol, and 3.6 to -0.2 kJ/mol at positions 2, 74, and 110, respectively. The identical substitution at different positions and different substitutions at the same position resulted in different degrees of stabilization. Changes in the stability of the mutant proteins could be evaluated by a unique equation considering the conformational changes due to the substitutions [Funahashi et al. (1999) Protein Eng. 12, 841-850]. For this calculation, secondary structural propensities were newly considered. However, some mutant proteins were not adapted to the equation. The hydration structures around the mutation sites of the exceptional mutant proteins were affected due to the substitutions. The stability changes in the exceptional mutant proteins could be explained by the formation or destruction of the hydration structures. These results suggest that the hydration structure mediated via hydrogen bonds covering the protein surface plays an important role in the conformational stability of the protein. Study holds ProTherm entries: 9650, 9651, 9652, 9653, 9654, 9655, 9656, 9657, 9658, 9659, 9660, 9661, 9662, 9663, 9664, 9665, 9666, 9667, 9668, 9669, 9670, 9671, 9672, 9673, 9674, 9675, 9676, 9677, 9678, 9679, 9680, 9681, 9682, 9683, 9684, 9685, 9686, 9687, 9688, 9689, 9690, 9691, 9692, 9693, 9694, 9695, 9696, 9697, 9698, 9699, 9700, 9701, 9702, 9703, 9704, 9705, 9706, 9707, 9708, 9709, 9710, 9711, 9712, 9713, 9714, 9715, 9716, 9717, 9718, 9719, 9720, 9721, 9722, 9724, 9725, 9726, 9727, 9728, 9730, 9731, 9732, 9733, 9734, 9735, 9736, 9737, 9738, 9739, 9740, 9741, 9742, 9743, 9744, 9745, 9746, 9747, 9748, 9749, 14497, 14498, 14499, 14500, 14501, 14502, 14503, 14504, 14505, 14506, 14507, 14508, 14509, 14510, 14511 Extra Details:

Submission Details

ID: i5k76m7B

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:38 p.m.

Version: 1

Publication Details
Funahashi J;Takano K;Yamagata Y;Yutani K,Biochemistry (2000) Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. PMID:11087397
Additional Information

Study Summary

Number of data points 226
Proteins Lysozyme C ; Lysozyme C ; Lysozyme C ; Lysozyme C ; Lysozyme C ; Lysozyme C ; Lysozyme C ; Lysozyme C ; Lysozyme C ; Lysozyme C ; Endoglucanase G ; Lysozyme C ; Beta-lactamase ; Lysozyme C ; Lysozyme C ; Lysozyme C ; Lysozyme C ; Lysozyme C
Unique complexes 16
Assays/Quantities/Protocols Experimental Assay: ddG ; Experimental Assay: dTm ; Experimental Assay: dCp ; Experimental Assay: dHcal pH:3.04 ; Experimental Assay: Tm pH:3.04 ; Experimental Assay: dHcal pH:2.72 ; Experimental Assay: Tm pH:2.72 ; Experimental Assay: dHcal pH:3.06 ; Experimental Assay: Tm pH:3.06 ; Experimental Assay: dHcal pH:2.85 ; Experimental Assay: Tm pH:2.85 ; Experimental Assay: dHcal pH:2.48 ; Experimental Assay: Tm pH:2.48 ; Experimental Assay: dHcal pH:3.25 ; Experimental Assay: Tm pH:3.25 ; Experimental Assay: dHcal pH:3.03 ; Experimental Assay: Tm pH:3.03 ; Experimental Assay: dHcal pH:2.82 ; Experimental Assay: Tm pH:2.82 ; Experimental Assay: dHcal pH:2.9 ; Experimental Assay: Tm pH:2.9 ; Experimental Assay: dHcal pH:3.11 ; Experimental Assay: Tm pH:3.11 ; Experimental Assay: dHcal pH:2.6 ; Experimental Assay: Tm pH:2.6 ; Experimental Assay: dHcal pH:3.23 ; Experimental Assay: Tm pH:3.23 ; Experimental Assay: dHcal pH:2.84 ; Experimental Assay: Tm pH:2.84 ; Experimental Assay: dHcal pH:3.2 ; Experimental Assay: Tm pH:3.2 ; Experimental Assay: dHcal pH:3.1 ; Experimental Assay: Tm pH:3.1 ; Experimental Assay: dHcal pH:3.15 ; Experimental Assay: Tm pH:3.15 ; Experimental Assay: dHcal pH:3.0 ; Experimental Assay: Tm pH:3.0 ; Experimental Assay: dHcal pH:2.8 ; Experimental Assay: Tm pH:2.8 ; Experimental Assay: dHcal pH:2.67 ; Experimental Assay: Tm pH:2.67 ; Experimental Assay: dHcal pH:3.3 ; Experimental Assay: Tm pH:3.3 ; Experimental Assay: dHcal pH:2.95 ; Experimental Assay: Tm pH:2.95 ; Experimental Assay: dHcal pH:2.78 ; Experimental Assay: Tm pH:2.78 ; Experimental Assay: dHcal pH:2.53 ; Experimental Assay: Tm pH:2.53 ; Experimental Assay: dHcal pH:3.22 ; Experimental Assay: Tm pH:3.22 ; Experimental Assay: dHcal pH:2.87 ; Experimental Assay: Tm pH:2.87 ; Experimental Assay: dHcal pH:2.68 ; Experimental Assay: Tm pH:2.68 ; Experimental Assay: dHcal pH:3.31 ; Experimental Assay: Tm pH:3.31 ; Experimental Assay: dHcal pH:3.09 ; Experimental Assay: Tm pH:3.09 ; Experimental Assay: dHcal pH:2.94 ; Experimental Assay: Tm pH:2.94 ; Experimental Assay: dHcal pH:2.73 ; Experimental Assay: Tm pH:2.73 ; Experimental Assay: dHcal pH:2.52 ; Experimental Assay: Tm pH:2.52 ; Experimental Assay: dHcal pH:3.05 ; Experimental Assay: Tm pH:3.05 ; Experimental Assay: dHcal pH:2.49 ; Experimental Assay: Tm pH:2.49 ; Experimental Assay: dHcal pH:3.13 ; Experimental Assay: Tm pH:3.13 ; Experimental Assay: dHcal pH:2.92 ; Experimental Assay: Tm pH:2.92 ; Experimental Assay: dHcal pH:2.7 ; Experimental Assay: Tm pH:2.7 ; Experimental Assay: dHcal pH:2.5 ; Experimental Assay: Tm pH:2.5 ; Experimental Assay: dHcal pH:3.4 ; Experimental Assay: Tm pH:3.4 ; Experimental Assay: dHcal pH:3.19 ; Experimental Assay: Tm pH:3.19 ; Experimental Assay: dHcal pH:3.08 ; Experimental Assay: Tm pH:3.08 ; Experimental Assay: dHcal pH:2.83 ; Experimental Assay: Tm pH:2.83 ; Experimental Assay: dHcal pH:2.65 ; Experimental Assay: Tm pH:2.65
Libraries Mutations for sequence KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV

Structure view and single mutant data analysis

Study data

No weblogo for data of varying length.
Colors: D E R H K S T N Q A V I L M F Y W C G P
 

Data Distribution

Studies with similar sequences (approximate matches)

Correlation with other assays (exact sequence matches)


Relevant PDB Entries

Structure ID Release Date Resolution Structure Title
1IY4 2002-07-31 Solution structure of the human lysozyme at 35 degree C
1IY3 2002-07-31 Solution Structure of the Human lysozyme at 4 degree C
2NWD 2006-12-19 1.04 Structure of chemically synthesized human lysozyme at 1 Angstrom resolution
5LSH 2017-06-21 1.06 human lysozyme in complex with a tetrasaccharide fragment of the O-chain of LPS from Klebsiella pneumoniae
1JSF 1998-04-29 1.15 FULL-MATRIX LEAST-SQUARES REFINEMENT OF HUMAN LYSOZYME
1RGZ 2004-04-06 1.37 Enterobacter cloacae GC1 Class C beta-Lactamase Complexed with Transition-State Analog of Cefotaxime
1IWY 2002-09-04 1.4 Crystal Structure Analysis of Human lysozyme at 170K.
1IWV 2002-09-04 1.4 Crystal Structure Analysis of Human lysozyme at 147K.
1IWU 2002-09-04 1.4 Crystal Structure Analysis of Human lysozyme at 127K.
1JWR 2001-09-19 1.4 Crystal structure of human lysozyme at 100 K
1IWW 2002-09-04 1.4 Crystal Structure Analysis of Human lysozyme at 152K.
1IWT 2002-09-04 1.4 Crystal Structure Analysis of Human lysozyme at 113K.
1IWX 2002-09-04 1.4 Crystal Structure Analysis of Human lysozyme at 161K.
1IWZ 2002-09-04 1.48 Crystal Structure Analysis of Human lysozyme at 178K.
1REX 1997-02-12 1.5 NATIVE HUMAN LYSOZYME
1LZR 1995-04-20 1.5 STRUCTURAL CHANGES OF THE ACTIVE SITE CLEFT AND DIFFERENT SACCHARIDE BINDING MODES IN HUMAN LYSOZYME CO-CRYSTALLIZED WITH HEXA-N-ACETYL-CHITOHEXAOSE AT PH 4.0
3FE0 2009-12-08 1.5 X-ray crystal structure of wild type human lysozyme in D2O
1LZ1 1985-01-02 1.5 REFINEMENT OF HUMAN LYSOZYME AT 1.5 ANGSTROMS RESOLUTION. ANALYSIS OF NON-BONDED AND HYDROGEN-BOND INTERACTIONS
4R0P 2014-12-17 1.52 Ifqins, an amyloid forming segment from human lysozyme spanning residues 56-61
1LMT 1995-03-31 1.6 STRUCTURE OF A CONFORMATIONALLY CONSTRAINED ARG-GLY-ASP SEQUENCE INSERTED INTO HUMAN LYSOZYME
1LZS 1995-04-20 1.6 STRUCTURAL CHANGES OF THE ACTIVE SITE CLEFT AND DIFFERENT SACCHARIDE BINDING MODES IN HUMAN LYSOZYME CO-CRYSTALLIZED WITH HEXA-N-ACETYL-CHITOHEXAOSE AT PH 4.0
1G87 2003-07-15 1.6 THE CRYSTAL STRUCTURE OF ENDOGLUCANASE 9G FROM CLOSTRIDIUM CELLULOLYTICUM
1JKC 1997-05-15 1.6 HUMAN LYSOZYME MUTANT WITH TRP 109 REPLACED BY PHE
1JKA 1997-05-15 1.66 HUMAN LYSOZYME MUTANT WITH GLU 35 REPLACED BY ASP
1JKB 1997-05-15 1.66 HUMAN LYSOZYME MUTANT WITH GLU 35 REPLACED BY ALA
1REZ 1997-02-12 1.7 HUMAN LYSOZYME-N-ACETYLLACTOSAMINE COMPLEX
1TCY 1993-01-15 1.7 DISSECTION OF THE FUNCTIONAL ROLE OF STRUCTURAL ELEMENTS OF TYROSINE-63 IN THE CATALYTIC ACTION OF HUMAN LYSOZYME
1REY 1997-02-12 1.7 HUMAN LYSOZYME-N,N'-DIACETYLCHITOBIOSE COMPLEX
1TAY 1993-01-15 1.7 DISSECTION OF THE FUNCTIONAL ROLE OF STRUCTURAL ELEMENTS OF TYROSINE-63 IN THE CATALYTIC ACTION OF HUMAN LYSOZYME
1GA2 2003-07-22 1.7 THE CRYSTAL STRUCTURE OF ENDOGLUCANASE 9G FROM CLOSTRIDIUM CELLULOLYTICUM COMPLEXED WITH CELLOBIOSE
1GE1 2000-11-08 1.7 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT LEFT-HANDED HELICAL POSITIONS
1TDY 1993-01-15 1.7 DISSECTION OF THE FUNCTIONAL ROLE OF STRUCTURAL ELEMENTS OF TYROSINE-63 IN THE CATALYTIC ACTION OF HUMAN LYSOZYME
4XUX 2015-04-01 1.75 Structure of ampC bound to RPX-7009 at 1.75 A
1LAA 1993-01-15 1.77 X-RAY STRUCTURE OF GLU 53 HUMAN LYSOZYME
1TBY 1993-01-15 1.77 DISSECTION OF THE FUNCTIONAL ROLE OF STRUCTURAL ELEMENTS OF TYROSINE-63 IN THE CATALYTIC ACTION OF HUMAN LYSOZYME
133L 1993-10-31 1.77 ROLE OF ARG 115 IN THE CATALYTIC ACTION OF HUMAN LYSOZYME. X-RAY STRUCTURE OF HIS 115 AND GLU 115 MUTANTS
134L 1993-10-31 1.77 ROLE OF ARG 115 IN THE CATALYTIC ACTION OF HUMAN LYSOZYME. X-RAY STRUCTURE OF HIS 115 AND GLU 115 MUTANTS
1IP4 2001-11-14 1.8 G72A HUMAN LYSOZYME
1CKD 1999-04-30 1.8 T43V MUTANT HUMAN LYSOZYME
1YAN 1996-04-03 1.8 CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: CALORIMETRIC STUDIES AND X-RAY STRUCTURAL ANALYSIS OF THE FIVE ISOLEUCINE TO VALINE MUTANTS
1EQ5 2000-04-19 1.8 CRYSTAL STRUCTURES OF SALT BRIDGE MUTANTS OF HUMAN LYSOZYME
1HNL 1995-02-14 1.8 CRYSTAL STRUCTURE OF A GLUTATHIONYLATED HUMAN LYSOZYME: A FOLDING INTERMEDIATE MIMIC IN THE FORMATION OF A DISULFIDE BOND
1LHI 1994-01-31 1.8 ROLE OF PROLINE RESIDUES IN HUMAN LYSOZYME STABILITY: A SCANNING CALORIMETRIC STUDY COMBINED WITH X-RAY STRUCTURE ANALYSIS OF PROLINE MUTANTS
1OUE 1997-02-12 1.8 CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V125A MUTANT
1LOZ 1997-04-01 1.8 AMYLOIDOGENIC VARIANT (I56T) VARIANT OF HUMAN LYSOZYME
1EQE 2000-04-19 1.8 CRYSTAL STRUCTURES OF SALT BRIDGE MUTANTS OF HUMAN LYSOZYME
1CJ6 1999-04-30 1.8 T11A MUTANT HUMAN LYSOZYME
2HED 1998-01-14 1.8 CONTRIBUTION OF WATER MOLECULES IN THE INTERIOR OF A PROTEIN TO THE CONFORMATIONAL STABILITY
2BQM 1998-08-12 1.8 CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
1GAZ 2000-07-27 1.8 Crystal Structure of Mutant Human Lysozyme Substituted at the Surface Positions
1B7R 1999-02-02 1.8 VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES
1I1Z 2001-02-28 1.8 MUTANT HUMAN LYSOZYME (Q86D)
1GF0 2001-04-18 1.8 BURIED POLAR MUTANT HUMAN LYSOZYME
1LHK 1994-01-31 1.8 ROLE OF PROLINE RESIDUES IN HUMAN LYSOZYME STABILITY: A SCANNING CALORIMETRIC STUDY COMBINED WITH X-RAY STRUCTURE ANALYSIS OF PROLINE MUTANTS
3LHM 1992-04-15 1.8 CRYSTAL STRUCTURES OF THE APO-AND HOLOMUTANT HUMAN LYSOZYMES WITH AN INTRODUCED CA2+ BINDING SITE
1GF7 2001-04-18 1.8 BURIED POLAR MUTANT HUMAN LYSOZYME
2ZIL 2009-01-06 1.8 Crystal Structure of Human Lysozyme from Urine
1GFR 2000-12-27 1.8 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
1I22 2001-02-28 1.8 MUTANT HUMAN LYSOZYME (A83K/Q86D/A92D)
2BQO 1998-08-12 1.8 CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
1GFJ 2000-12-20 1.8 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
1LHJ 1994-01-31 1.8 ROLE OF PROLINE RESIDUES IN HUMAN LYSOZYME STABILITY: A SCANNING CALORIMETRIC STUDY COMBINED WITH X-RAY STRUCTURE ANALYSIS OF PROLINE MUTANTS
2BQG 1998-08-12 1.8 CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
2HEA 1998-01-14 1.8 CONTRIBUTION OF WATER MOLECULES IN THE INTERIOR OF A PROTEIN TO THE CONFORMATIONAL STABILITY
1GB0 2000-07-27 1.8 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
1B7N 1999-01-27 1.8 VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES
1OUH 1997-02-12 1.8 CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V74A MUTANT
1GF8 2000-12-20 1.8 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
1GB9 2000-07-27 1.8 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
1YAP 1996-04-03 1.8 CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: CALORIMETRIC STUDIES AND X-RAY STRUCTURAL ANALYSIS OF THE FIVE ISOLEUCINE TO VALINE MUTANTS
1YAQ 1996-04-03 1.8 CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: CALORIMETRIC STUDIES AND X-RAY STRUCTURAL ANALYSIS OF THE FIVE ISOLEUCINE TO VALINE MUTANTS
1GF4 2001-04-18 1.8 BURIED POLAR MUTANT HUMAN LYSOZYME
1GBX 2000-07-27 1.8 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
1GE0 2000-11-08 1.8 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT LEFT-HANDED HELICAL POSITIONS
1GFK 2000-12-20 1.8 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
1GB5 2000-07-27 1.8 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
1GCE 1999-08-27 1.8 STRUCTURE OF THE BETA-LACTAMASE OF ENTEROBACTER CLOACAE GC1
1WQN 1998-07-01 1.8 CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
2HEE 1998-01-14 1.8 CONTRIBUTION OF WATER MOLECULES IN THE INTERIOR OF A PROTEIN TO THE CONFORMATIONAL STABILITY
1LZ5 1993-10-31 1.8 STRUCTURAL AND FUNCTIONAL ANALYSES OF THE ARG-GLY-ASP SEQUENCE INTRODUCED INTO HUMAN LYSOZYME
2BQB 1998-08-12 1.8 CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
2BQF 1998-08-12 1.8 CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
1CJ9 1999-04-30 1.8 T40V MUTANT HUMAN LYSOZYME
1GFU 2000-12-27 1.8 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
1GDX 2000-11-08 1.8 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT LEFT-HANDED HELICAL POSITIONS
2MED 1998-07-15 1.8 CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
1B7O 1999-02-02 1.8 VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES
1GBW 2000-07-27 1.8 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
1LYY 1997-04-01 1.8 AMYLOIDOGENIC VARIANT (ASP67HIS) OF HUMAN LYSOZYME
1IP3 2001-11-14 1.8 G68A HUMAN LYSOZYME
1C45 1999-08-20 1.8 MUTANT HUMAN LYSOZYME WITH FOREIGN N-TERMINAL RESIDUES
1YAO 1996-04-03 1.8 CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: CALORIMETRIC STUDIES AND X-RAY STRUCTURAL ANALYSIS OF THE FIVE ISOLEUCINE TO VALINE MUTANTS
1GDW 2000-11-01 1.8 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT LEFT-HANDED HELICAL POSITIONS
1INU 2000-12-20 1.8 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
1LZ6 1993-10-31 1.8 STRUCTURAL AND FUNCTIONAL ANALYSES OF THE ARG-GLY-ASP SEQUENCE INTRODUCED INTO HUMAN LYSOZYME
1OUF 1997-02-12 1.8 CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V130A MUTANT
1GAY 2000-06-29 1.8 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
1CKC 1999-04-30 1.8 T43A MUTANT HUMAN LYSOZYME
5XHR 2017-09-27 1.8 Crystal structure of P99 beta-lactamase in complex with a penicillin derivative MPC-1
207L 1996-10-14 1.8 MUTANT HUMAN LYSOZYME C77A
1GBZ 2000-07-27 1.8 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
1GFG 2000-12-20 1.8 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
1IP6 2001-11-14 1.8 G127A HUMAN LYSOZYME
1GB6 2000-07-27 1.8 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
4ML7 2014-07-23 1.8 Crystal structure of Brucella abortus PliC in complex with human lysozyme
1CKF 1999-04-30 1.8 T52A MUTANT HUMAN LYSOZYME
1B7L 1999-01-27 1.8 VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES
1GB3 2000-07-27 1.8 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
1JKD 1997-05-15 1.8 HUMAN LYSOZYME MUTANT WITH TRP 109 REPLACED BY ALA
2BQH 1998-08-12 1.8 CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
2BQN 1998-08-12 1.8 CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
2MEB 1998-07-15 1.8 CHANGES IN CONFORMATIONAL STABILITY OF A SERIES OF MUTANT HUMAN LYSOZYMES AT CONSTANT POSITIONS
1OUB 1997-02-12 1.8 CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V100A MUTANT
2BQD 1998-08-12 1.8 CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
1OUA 1997-02-12 1.8 CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE I56T MUTANT
1GB8 2000-07-27 1.8 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
1C43 1999-08-20 1.8 MUTANT HUMAN LYSOZYME WITH FOREIGN N-TERMINAL RESIDUES
1B5U 1999-01-20 1.8 CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME: CALORIMETRY AND X-RAY ANALYSIS OF SIX SER->ALA MUTANT
1WQQ 1998-07-01 1.8 CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
2MEE 1998-07-15 1.8 CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
1IP2 2001-11-14 1.8 G48A HUMAN LYSOZYME
1OUJ 1997-02-12 1.8 CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V99A MUTANT
1OUG 1997-02-12 1.8 CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V2A MUTANT
1IP1 2001-11-14 1.8 G37A HUMAN LYSOZYME
2BQL 1998-08-12 1.8 CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
1GF5 2001-04-18 1.8 BURIED POLAR MUTANT HUMAN LYSOZYME
1GF3 2001-04-18 1.8 BURIED POLAR MUTANT HUMAN LYSOZYME
1GE4 2000-11-08 1.8 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT LEFT-HANDED HELICAL POSITIONS
1WQM 1998-07-01 1.8 CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
1OUD 1997-02-12 1.8 CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V121A MUTANT
2BQC 1998-08-12 1.8 CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
1EQ4 2000-04-19 1.8 CRYSTAL STRUCTURES OF SALT BRIDGE MUTANTS OF HUMAN LYSOZYME
1GBY 2000-07-27 1.8 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
1WQP 1998-07-01 1.8 CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
1GBO 2000-07-27 1.8 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
2BQA 1998-08-12 1.8 CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
1WQO 1998-07-01 1.8 CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
1IX0 2003-07-22 1.8 I59A-3SS human lysozyme
1WQR 1998-07-01 1.8 CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
1GFV 2000-12-27 1.8 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
2LHM 1992-04-15 1.8 CRYSTAL STRUCTURES OF THE APO-AND HOLOMUTANT HUMAN LYSOZYMES WITH AN INTRODUCED CA2+ BINDING SITE
1GB7 2000-07-27 1.8 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
1CJ7 1999-04-30 1.8 T11V MUTANT HUMAN LYSOZYME
1GE3 2000-11-08 1.8 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT LEFT-HANDED HELICAL POSITIONS
1GFA 2000-12-20 1.8 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
1OUC 1997-02-12 1.8 CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V110A MUTANT
2MEH 1998-07-15 1.8 CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
1OUI 1997-02-12 1.8 CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V93A MUTANT
2BQE 1998-08-12 1.8 CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
1GFE 2000-12-20 1.8 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
1DI3 1999-12-08 1.8 ROLE OF AMINO ACID RESIDUES AT TURNS IN THE CONFORMATIONAL STABILITY AND FOLDING OF HUMAN LYSOZYME
1LHM 1992-04-15 1.8 THE CRYSTAL STRUCTURE OF A MUTANT LYSOZYME C77(SLASH)95A WITH INCREASED SECRETION EFFICIENCY IN YEAST
1LHL 1994-01-31 1.8 ROLE OF PROLINE RESIDUES IN HUMAN LYSOZYME STABILITY: A SCANNING CALORIMETRIC STUDY COMBINED WITH X-RAY STRUCTURE ANALYSIS OF PROLINE MUTANTS
1LZ4 1993-10-31 1.8 ENTHALPIC DESTABILIZATION OF A MUTANT HUMAN LYSOZYME LACKING A DISULFIDE BRIDGE BETWEEN CYSTEINE-77 AND CYSTEINE-95
1GFH 2000-12-20 1.8 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
2BQI 1998-08-12 1.8 CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
1LHH 1994-01-31 1.8 ROLE OF PROLINE RESIDUES IN HUMAN LYSOZYME STABILITY: A SCANNING CALORIMETRIC STUDY COMBINED WITH X-RAY STRUCTURE ANALYSIS OF PROLINE MUTANTS
2BQK 1998-08-12 1.8 CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
1IP5 2001-11-14 1.8 G105A HUMAN LYSOZYME
1K72 2003-07-15 1.8 The X-ray Crystal Structure Of Cel9G Complexed With cellotriose
1GEZ 2001-04-18 1.8 BURIED POLAR MUTANT HUMAN LYSOZYME
2HEC 1998-01-14 1.8 CONTRIBUTION OF WATER MOLECULES IN THE INTERIOR OF A PROTEIN TO THE CONFORMATIONAL STABILITY
2MEI 1998-07-15 1.8 CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
1YAM 1996-04-03 1.8 CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: CALORIMETRIC STUDIES AND X-RAY STRUCTURAL ANALYSIS OF THE FIVE ISOLEUCINE TO VALINE MUTANTS
1CJ8 1999-04-30 1.8 T40A MUTANT HUMAN LYSOZYME
2MEG 1998-07-15 1.8 CHANGES IN CONFORMATIONAL STABILITY OF A SERIES OF MUTANT HUMAN LYSOZYMES AT CONSTANT POSITIONS.
1GB2 2000-07-27 1.8 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
2ZWB 2009-12-08 1.8 Neutron crystal structure of wild type human lysozyme in D2O
2BQJ 1998-08-12 1.8 CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
2MEF 1998-07-15 1.8 CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
2HEF 1998-01-14 1.8 CONTRIBUTION OF WATER MOLECULES IN THE INTERIOR OF A PROTEIN TO THE CONFORMATIONAL STABILITY
1GFT 2000-12-27 1.8 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
1GF6 2001-04-18 1.8 BURIED POLAR MUTANT HUMAN LYSOZYME
1GF9 2000-12-20 1.8 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
2ZIK 2009-01-06 1.81 Crystal Structure of Human Lysozyme from Pichia pastoris
3EBA 2008-12-02 1.85 CAbHul6 FGLW mutant (humanized) in complex with human lysozyme
1QSW 2001-08-08 1.85 CRYSTAL STRUCTURE ANALYSIS OF A HUMAN LYSOZYME MUTANT W64C C65A
1OP9 2003-10-14 1.86 Complex of human lysozyme with camelid VHH HL6 antibody fragment
1XX2 2004-11-23 1.88 Refinement of P99 beta-lactamase from Enterobacter cloacae
1IP7 2001-11-14 1.9 G129A HUMAN LYSOZYME
1KFG 2003-07-15 1.9 The X-ray Crystal Structure of Cel9G from Clostridium cellulolyticum complexed with a Thio-Oligosaccharide Inhibitor
1I20 2001-02-28 1.9 MUTANT HUMAN LYSOZYME (A92D)
2ZIJ 2009-01-06 1.9 Crystal Structure of Human Lysozyme Expressed in E. coli.
3S4X 2012-08-01 1.95 Crystal structure of the Asn152Gly mutant of P99 beta-lactamase
4I0C 2013-10-09 1.95 The structure of the camelid antibody cAbHuL5 in complex with human lysozyme
1D6Q 2000-01-21 1.96 HUMAN LYSOZYME E102 MUTANT LABELLED WITH 2',3'-EPOXYPROPYL GLYCOSIDE OF N-ACETYLLACTOSAMINE
1B5X 1999-01-20 2.0 Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and x-ray analysis of six ser->ala mutants
1B7Q 1999-02-02 2.0 VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES
1UBZ 2003-04-22 2.0 Crystal structure of Glu102-mutant human lysozyme doubly labeled with 2',3'-epoxypropyl beta-glycoside of N-acetyllactosamine
1GE2 2000-11-08 2.0 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT LEFT-HANDED HELICAL POSITIONS
1DI4 1999-12-08 2.0 ROLE OF AMINO ACID RESIDUES AT TURNS IN THE CONFORMATIONAL STABILITY AND FOLDING OF HUMAN LYSOZYME
1CKH 1999-04-30 2.0 T70V MUTANT HUMAN LYSOZYME
1B7P 1999-01-25 2.0 VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES
1B7S 1999-02-02 2.0 VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES
3LN2 2011-02-16 2.04 Crystal Structure of a Charge Engineered Human Lysozyme Variant
2Q9M 2007-08-21 2.05 4-Substituted Trinems as Broad Spectrum-Lactamase Inhibitors: Structure-based Design, Synthesis and Biological Activity
1REM 1998-07-15 2.1 HUMAN LYSOZYME WITH MAN-B1,4-GLCNAC COVALENTLY ATTACHED TO ASP53
1Y54 2005-03-29 2.1 Crystal structure of the native class C beta-lactamase from Enterobacter cloacae 908R complexed with BRL42715
1GEV 2001-04-18 2.1 BURIED POLAR MUTANT HUMAN LYSOZYME
1B5V 1999-01-20 2.17 CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME: CALORIMETRY AND X-RAY ANALYSIS OF SIX SER->ALA MUTANTS
1B5W 1999-01-20 2.17 CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME: CALORIMETRY AND X-RAY ANALYSIS OF SIX SER->ALA MUTANTS
2HEB 1998-01-28 2.2 CONTRIBUTION OF WATER MOLECULES IN THE INTERIOR OF A PROTEIN TO THE CONFORMATIONAL STABILITY
2MEA 1998-07-15 2.2 CHANGES IN CONFORMATIONAL STABILITY OF A SERIES OF MUTANT HUMAN LYSOZYMES AT CONSTANT POSITIONS
1C46 1999-08-20 2.2 MUTANT HUMAN LYSOZYME WITH FOREIGN N-TERMINAL RESIDUES
1B5Z 1999-02-02 2.2 CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME: CALORIMETRY AND X-RAY ANALYSIS OF SIX SER->ALA MUTANTS
1CKG 1999-05-05 2.2 T52V MUTANT HUMAN LYSOZYME
2MEC 1998-07-15 2.2 CHANGES IN CONFORMATIONAL STABILITY OF A SERIES OF MUTANT HUMAN LYSOZYMES AT CONSTANT POSITIONS
1B7M 1999-01-27 2.2 VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES
1B5Y 1999-01-20 2.2 CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME: CALORIMETRY AND X-RAY ANALYSIS OF SIX SER->ALA MUTANTS
208L 1996-10-14 2.2 MUTANT HUMAN LYSOZYME C77A
1DI5 1999-12-08 2.2 ROLE OF AMINO ACID RESIDUES AT TURNS IN THE CONFORMATIONAL STABILITY AND FOLDING OF HUMAN LYSOZYME
2Q9N 2007-08-21 2.2 4-Substituted Trinems as Broad Spectrum-Lactamase Inhibitors: Structure-based Design, Synthesis and Biological Activity
1D6P 2000-01-21 2.23 HUMAN LYSOZYME L63 MUTANT LABELLED WITH 2',3'-EPOXYPROPYL N,N'-DIACETYLCHITOBIOSE
1BLS 1995-05-08 2.3 CRYSTALLOGRAPHIC STRUCTURE OF A PHOSPHONATE DERIVATIVE OF THE ENTEROBACTER CLOACAE P99 CEPHALOSPORINASE: MECHANISTIC INTERPRETATION OF A BETA-LACTAMASE TRANSITION STATE ANALOG
1RE2 1999-05-05 2.3 HUMAN LYSOZYME LABELLED WITH TWO 2',3'-EPOXYPROPYL BETA-GLYCOSIDE OF N-ACETYLLACTOSAMINE
1IOC 2002-10-09 2.4 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME, EAEA-I56T
1C7P 2000-04-05 2.4 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME WITH FOUR EXTRA RESIDUES (EAEA) AT THE N-TERMINAL
5LVK 2016-09-28 2.49 Human Lysozyme soaked with [H2Ind][trans-RuCl4(DMSO)(HInd)]
1W08 2004-06-10 2.5 STRUCTURE OF T70N HUMAN LYSOZYME
5HAI 2016-09-07 2.74 P99 beta-lactamase mutant - S64G

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
96.9 Lysozyme C P79180 LYSC_HYLLA
99.2 Lysozyme C P79239 LYSC_PONPY
100.0 Lysozyme C P79179 LYSC_GORGO
100.0 Lysozyme C P61628 LYSC_PANTR
100.0 Lysozyme C P61627 LYSC_PANPA
100.0 Lysozyme C P61626 LYSC_HUMAN
90.8 Lysozyme C P61634 LYSC_ERYPA
90.8 Lysozyme C P61633 LYSC_CHLAE
100.0 Endoglucanase G P37700 GUNG_CLOCE
98.6 Beta-lactamase P05364 AMPC_ENTCL