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1OVK

T4 Lysozyme Cavity Mutant L99A/M102Q Bound with N-Allyl-Aniline

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0003824molecular_functioncatalytic activity
A0008152biological_processmetabolic process
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 Residues3
DetailsBINDING SITE FOR RESIDUE CL A 173
ChainResidue
AASN144
AARG145
AHOH291

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CL A 178
ChainResidue
AALA49
AGLN69
ASER136
AARG137
AASN140
AHOH282

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE BME A 168
ChainResidue
AASP72
AVAL75
AARG76
ALEU79
ATYR88
ABME170

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE BME A 169
ChainResidue
AGLY30
APHE104
AHOH256
AHOH274

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE BME A 170
ChainResidue
AASP72
ABME168
AHOH199

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE NYL A 405
ChainResidue
ATYR88
AALA99
AGLN102
AVAL103
AVAL111
ASER117
ALEU118
ALEU121
APHE153

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098
ChainResidueDetails
AGLU11

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:1892846, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098
ChainResidueDetails
AASP20

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:8266098
ChainResidueDetails
ALEU32
APHE104

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000303|PubMed:7831309
ChainResidueDetails
ASER117
AASN132

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

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PDB entries from 2024-04-10

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