1AF2
CRYSTAL STRUCTURE OF CYTIDINE DEAMINASE COMPLEXED WITH URIDINE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001884 | molecular_function | pyrimidine nucleoside binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004126 | molecular_function | cytidine deaminase activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006217 | biological_process | deoxycytidine catabolic process |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0009972 | biological_process | obsolete cytidine deamination |
| A | 0015949 | biological_process | nucleobase-containing small molecule interconversion |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046135 | biological_process | pyrimidine nucleoside catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 296 |
| Chain | Residue |
| A | HIS102 |
| A | CYS129 |
| A | CYS132 |
| A | U5P295 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE U5P A 295 |
| Chain | Residue |
| A | ASN89 |
| A | GLU91 |
| A | THR100 |
| A | VAL101 |
| A | HIS102 |
| A | ALA103 |
| A | GLU104 |
| A | PRO128 |
| A | CYS129 |
| A | CYS132 |
| A | PHE165 |
| A | ALA231 |
| A | ZN296 |
| A | HOH617 |
| A | PHE71 |
| site_id | ZN |
| Number of Residues | 4 |
| Details | ZN BINDING SITE. |
| Chain | Residue |
| A | HIS102 |
| A | CYS129 |
| A | CYS132 |
| A | U5P295 |
Functional Information from PROSITE/UniProt
| site_id | PS00903 |
| Number of Residues | 35 |
| Details | CYT_DCMP_DEAMINASES_1 Cytidine and deoxycytidylate deaminases zinc-binding region signature. HAEqsAIshawlsgekalaaitvnyt..............PCgh......CrqfM |
| Chain | Residue | Details |
| A | HIS102-MET136 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 120 |
| Details | Domain: {"description":"CMP/dCMP-type deaminase 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01083","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 108 |
| Details | Domain: {"description":"CMP/dCMP-type deaminase 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU01083","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"8289286","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"8634261","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"9125497","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"8289286","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"8634261","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"9125497","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ctt |
| Chain | Residue | Details |
| A | GLU104 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 97 |
| Chain | Residue | Details |
| A | HIS102 | metal ligand |
| A | GLU104 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | CYS129 | metal ligand |
| A | CYS132 | metal ligand |
