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3DN4

Iodobenzene binding in the hydrophobic cavity of T4 lysozyme L99A mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0009253biological_processpeptidoglycan catabolic process
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 Residues9
DetailsBINDING SITE FOR RESIDUE PO4 A 901
ChainResidue
AARG14
ALYS19
AARG125
ATRP126
AASP127
AGLU128
AHOH908
AHOH1072
AHOH1077

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 A 902
ChainResidue
AGLN122
AASN144
AARG148
AHOH923
AHOH1032
AHOH1036
AHOH1089

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PIH A 900
ChainResidue
ALEU84
ATYR88
AALA99
AMET102
ALEU118
APHE153

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE HED A 903
ChainResidue
AASN68
AASP72
AALA93
AARG96
AILE100

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HED A 904
ChainResidue
AASP72
AARG76
ALEU79
ATYR88

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE HED A 905
ChainResidue
AGLY30
AHIS31
ALEU32
AASP70
APHE104
AHOH1031
AHOH1114

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_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 2024-07-10

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