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188L

SPECIFICITY OF LIGAND BINDING IN A BURIED NON-POLAR CAVITY OF T4 LYSOZYME: LINKAGE OF DYNAMICS AND STRUCTURAL PLASTICITY

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_id99A
Number of Residues17
Details
ChainResidue
AILE78
AVAL111
AALA112
AGLY113
APHE114
ALEU118
ALEU121
ALEU133
APHE153
ALEU84
AVAL87
ATYR88
AALA99
AMET102
AVAL103
ATHR109
AGLY110

site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CL A 173
ChainResidue
ALYS124
ATHR142
AASN144
AARG145
AHOH209
AHOH291

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 178
ChainResidue
ALYS135
AHOH215

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HED A 170
ChainResidue
AASN68
AASP72
AALA93
AILE100

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE OXE A 400
ChainResidue
ALEU84
AALA99
AMET102
AVAL103
AVAL111
ALEU118

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 2024-03-27

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