1K6W
The Structure of Escherichia coli Cytosine Deaminase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004131 | molecular_function | cytosine deaminase activity |
A | 0005829 | cellular_component | cytosol |
A | 0006209 | biological_process | cytosine catabolic process |
A | 0008198 | molecular_function | ferrous iron binding |
A | 0008270 | molecular_function | zinc ion binding |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
A | 0016814 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines |
A | 0019239 | molecular_function | deaminase activity |
A | 0019858 | biological_process | cytosine metabolic process |
A | 0035888 | molecular_function | isoguanine deaminase activity |
A | 0042802 | molecular_function | identical protein binding |
A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FE A 501 |
Chain | Residue |
A | HIS61 |
A | HIS63 |
A | HIS214 |
A | ASP313 |
A | HOH1000 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | Active 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"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | Binding 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."]}}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | Binding 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"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"11812140","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15381761","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21545144","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | Site: {"description":"Activates the nucleophilic water","evidences":[{"source":"PubMed","id":"21545144","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"21604715","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 710 |
Chain | Residue | Details |
A | HIS61 | metal ligand |
A | HIS63 | metal ligand |
A | GLN156 | electrostatic stabiliser |
A | HIS214 | metal ligand |
A | GLU217 | proton acceptor, proton donor |
A | ASP313 | metal ligand |