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3F9L

Evaulaution at Atomic Resolution of the Role of Strain in Destabilizing the Temperature Sensitive T4 Lysozyme Mutant Arg96-->His

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 166
ChainResidue
AARG14
ALYS19
AARG125
ATRP126
AASP127
AGLU128
AHOH192
AHOH247
AHOH358

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 172
ChainResidue
AGLU11
ATYR18
AHOH204
AHOH207
AHOH263
AHOH304

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CL A 173
ChainResidue
ASER90
ALYS124
ATHR142
APRO143
AASN144
AARG145
AHOH209
AHOH214

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE K A 174
ChainResidue
AVAL57
AILE58
AHOH342
AHOH371

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 178
ChainResidue
AHIS31
ALYS135

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

221051

PDB entries from 2024-06-12

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