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2A4T

Crystal structure of spin labeled T4 Lysozyme (V131R7)

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 Residues3
DetailsBINDING SITE FOR RESIDUE R7A A 1131
ChainResidue
AARG80
AGLU108
ACYS131

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE AZI A 165
ChainResidue
AHOH241
AHOH301
ALYS19
AARG125
ATRP126
AASP127
AGLU128
AHOH222

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 166
ChainResidue
AGLU11
ATYR18
AHOH234
AHOH272
AHOH345

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CL A 167
ChainResidue
ALYS124
ATHR142
AASN144
AARG145
AHOH214
AHOH286

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 168
ChainResidue
AHIS31
ALYS135
AHOH266

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE HED A 169
ChainResidue
AASN68
AASP72
AVAL75
AVAL75
ATYR88
AALA93
AILE100
AHOH353

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

219140

PDB entries from 2024-05-01

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