3R0D
Crystal structure of Cytosine Deaminase from Escherichia Coli complexed with two zinc atoms in the active site
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 PXN A 427 |
| Chain | Residue |
| A | ASP98 |
| A | GLN102 |
| A | TRP105 |
| A | LYS109 |
| A | GLU420 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 428 |
| Chain | Residue |
| A | ZN429 |
| A | HOH434 |
| A | HIS61 |
| A | HIS63 |
| A | HIS214 |
| A | ASP313 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ZN A 429 |
| Chain | Residue |
| A | ASP313 |
| A | ASP314 |
| A | ZN428 |
| A | HOH433 |
| A | HOH434 |
| A | HOH435 |
| A | HOH436 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 430 |
| Chain | Residue |
| A | HIS97 |
| A | HIS97 |
| A | GLU138 |
| A | GLU138 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL A 431 |
| Chain | Residue |
| A | GLU49 |
| A | GLN50 |
| A | GLY51 |
| A | PRO380 |
| A | ALA381 |
| A | GLU382 |
| A | ASP386 |
| A | ARG390 |
| A | LYS425 |
| A | HOH579 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 432 |
| Chain | Residue |
| A | SER259 |
| A | GLU300 |
| A | HOH547 |
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 |
