Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

3DN4

Iodobenzene binding in the hydrophobic cavity of T4 lysozyme L99A mutant

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 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
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

246031

PDB entries from 2025-12-10

PDB statisticsPDBj update infoContact PDBjnumon