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1LWG

Multiple Methionine Substitutions are Tolerated in T4 Lysozyme and have Coupled Effects on Folding and Stability

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0003824molecular_functioncatalytic activity
A0009253biological_processpeptidoglycan catabolic process
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0016998biological_processcell wall macromolecule catabolic process
A0030430cellular_componenthost cell cytoplasm
A0031640biological_processkilling of cells of another organism
A0042742biological_processdefense response to bacterium
A0044659biological_processviral release from host cell by cytolysis
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 170
ChainResidue
ASER90
ATHR142
APRO143
AASN144
AARG145

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 227
ChainResidue
AHIS31
ALYS135
AHOH171
AHOH190

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 228
ChainResidue
ALYS65
AASN68
AVAL94
ATRP158

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K A 325
ChainResidue
AGLU11
AGLY12
ATYR18
AGLY28
AILE29
AGLY30

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 330
ChainResidue
ALYS65
AGLN69
AASP92
AALA93
AGLN141

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE HED A 901
ChainResidue
APHE4
AASP72
AVAL75
ATYR88
AALA93
AHOH174

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE HED A 902
ChainResidue
ALYS83
AMET111
ATHR115
AMET118
AARG119
AGLN122
AHOH513

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE HED A 903
ChainResidue
AILE9
AASP10
AGLU11
ATYR18
AGLN123
ALYS124
AHOH281
AHOH302

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_04110","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"3382407","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_04110","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1892846","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3382407","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 206l
ChainResidueDetails
AGLU11
AASP20

site_idMCSA1
Number of Residues2
DetailsM-CSA 921
ChainResidueDetails
AGLU11proton shuttle (general acid/base)
AASP20covalent catalysis

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PDB entries from 2025-08-27

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