1R9Y
Bacterial cytosine deaminase D314A mutant.
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 | 6 |
| Details | BINDING SITE FOR RESIDUE FE A 501 |
| Chain | Residue |
| A | HIS61 |
| A | HIS63 |
| A | HIS214 |
| A | ASP313 |
| A | MG502 |
| A | HOH604 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG A 502 |
| Chain | Residue |
| A | HOH603 |
| A | HOH604 |
| A | HOH605 |
| A | HOH606 |
| A | FE501 |
| A | HOH601 |
| A | HOH602 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 503 |
| Chain | Residue |
| A | ALA128 |
| A | LYS134 |
| A | GLU171 |
| A | ARG174 |
| A | LEU175 |
| A | HOH798 |
| A | HOH984 |
| A | HOH984 |
| A | HOH1026 |
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 |
