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1XJT

Crystal structure of active form of P1 phage endolysin Lyz

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
A0020002cellular_componenthost cell plasma membrane
A0031640biological_processkilling of cells of another organism
A0042742biological_processdefense response to bacterium
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE CIT A 192
ChainResidue
AILE21
AHOH386
AGLN94
AHIS95
AARG122
AHIS138
AGLN142
AHOH334
AHOH378
AHOH379

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CIT A 250
ChainResidue
ATYR124
ATHR135
ASER136
AASP155
AHOH285
AHOH354

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_04136","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15637279","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_04136","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15637279","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 206l
ChainResidueDetails
AGLU42
ACYS51

246031

PDB entries from 2025-12-10

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