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1K6W

The Structure of Escherichia coli Cytosine Deaminase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004131molecular_functioncytosine deaminase activity
A0005829cellular_componentcytosol
A0006209biological_processcytosine catabolic process
A0008198molecular_functionferrous iron binding
A0008270molecular_functionzinc ion binding
A0016787molecular_functionhydrolase activity
A0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
A0016814molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines
A0019239molecular_functiondeaminase activity
A0019858biological_processcytosine metabolic process
A0035888molecular_functionisoguanine deaminase activity
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE A 501
ChainResidue
AHIS61
AHIS63
AHIS214
AASP313
AHOH1000

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"11812140","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"21545144","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"21604715","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21545144","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21604715","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2011","submissionDatabase":"PDB data bank","title":"Crystal structure of cytosine deaminase from Escherichia coli complexed with two zinc atoms in the active site.","authors":["Fedorov A.A.","Fedorov E.V.","Kamat S.","Hitchcock D.","Raushel F.M.","Almo S.C."]}}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11812140","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15381761","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21545144","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21604715","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11812140","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15381761","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21545144","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsSite: {"description":"Activates the nucleophilic water","evidences":[{"source":"PubMed","id":"21545144","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"21604715","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 710
ChainResidueDetails
AHIS61metal ligand
AHIS63metal ligand
AGLN156electrostatic stabiliser
AHIS214metal ligand
AGLU217proton acceptor, proton donor
AASP313metal ligand

238582

PDB entries from 2025-07-09

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