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5JGV

Spin-Labeled T4 Lysozyme Construct A73V1

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 Residues3
Detailsbinding site for residue CL A 201
ChainResidue
AASN132
ALYS135
AHOH382

site_idAC2
Number of Residues6
Detailsbinding site for residue CL A 202
ChainResidue
ALYS124
ATHR142
AASN144
AARG145
AHOH345
AHOH530

site_idAC3
Number of Residues5
Detailsbinding site for residue K A 203
ChainResidue
AGLU11
ATYR18
AHOH398
AHOH440
AHOH487

site_idAC4
Number of Residues4
Detailsbinding site for residue CL A 204
ChainResidue
ALYS65
AGLN69
AALA93
AHOH363

site_idAC5
Number of Residues6
Detailsbinding site for residue CL A 205
ChainResidue
AALA49
AGLN69
ASER136
AARG137
AASN140
AHOH491

site_idAC6
Number of Residues5
Detailsbinding site for residue V1A A 206
ChainResidue
ACYS73
AARG80
ALYS135
ATYR139
AHOH312

site_idAC7
Number of Residues2
Detailsbinding site for residue CL A 207
ChainResidue
AARG52
AASN55

site_idAC8
Number of Residues5
Detailsbinding site for residue HEZ A 208
ChainResidue
AGLY30
ALEU32
AASP70
APHE104
AGLU108

site_idAC9
Number of Residues6
Detailsbinding site for residue HEZ A 209
ChainResidue
AASP47
AGLY51
AGLY110
AARG137
ATRP138
AHOH407

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_idMCSA1
Number of Residues2
DetailsM-CSA 921
ChainResidueDetails
AGLU11proton shuttle (general acid/base)
AASP20covalent catalysis

247536

PDB entries from 2026-01-14

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