1OX7
Crystal structure of yeast cytosine deaminase apo-enzyme: inorganic zinc bound
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004131 | molecular_function | cytosine deaminase activity |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0008655 | biological_process | pyrimidine-containing compound salvage |
| A | 0008835 | molecular_function | diaminohydroxyphosphoribosylaminopyrimidine deaminase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| 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 | 0044206 | biological_process | UMP salvage |
| A | 0046087 | biological_process | cytidine metabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0102480 | molecular_function | 5-fluorocytosine deaminase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004131 | molecular_function | cytosine deaminase activity |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0008655 | biological_process | pyrimidine-containing compound salvage |
| B | 0008835 | molecular_function | diaminohydroxyphosphoribosylaminopyrimidine deaminase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016814 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines |
| B | 0019239 | molecular_function | deaminase activity |
| B | 0019858 | biological_process | cytosine metabolic process |
| B | 0044206 | biological_process | UMP salvage |
| B | 0046087 | biological_process | cytidine metabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0102480 | molecular_function | 5-fluorocytosine deaminase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 400 |
| Chain | Residue |
| B | HIS262 |
| B | CYS291 |
| B | CYS294 |
| B | ZN403 |
| B | HOH507 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 401 |
| Chain | Residue |
| A | HOH551 |
| A | HOH552 |
| A | GLU64 |
| A | ZN402 |
| A | HOH549 |
| A | HOH550 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 402 |
| Chain | Residue |
| A | HIS62 |
| A | CYS91 |
| A | CYS94 |
| A | ZN401 |
| A | HOH550 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN B 403 |
| Chain | Residue |
| B | GLU264 |
| B | ZN400 |
| B | HOH504 |
| B | HOH506 |
| B | HOH507 |
| B | HOH508 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 404 |
| Chain | Residue |
| A | GLU75 |
| A | HOH774 |
| B | GLU328 |
| B | GLN350 |
| B | HOH519 |
| B | HOH576 |
Functional Information from PROSITE/UniProt
| site_id | PS00903 |
| Number of Residues | 37 |
| Details | CYT_DCMP_DEAMINASES_1 Cytidine and deoxycytidylate deaminases zinc-binding region signature. HGEisTLencgrlegkvykdttlyttls............PCdm......CtgaI |
| Chain | Residue | Details |
| A | HIS62-ILE98 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000269|PubMed:12637534, ECO:0007744|PDB:1UAQ |
| Chain | Residue | Details |
| A | GLU64 | |
| B | GLU264 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12637534, ECO:0000269|PubMed:12906827, ECO:0007744|PDB:1P6O, ECO:0007744|PDB:1UAQ |
| Chain | Residue | Details |
| A | ASN51 | |
| A | ASP155 | |
| B | ASN251 | |
| B | ASP355 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12637534, ECO:0000269|PubMed:12906827, ECO:0000269|PubMed:15879217, ECO:0007744|PDB:1OX7, ECO:0007744|PDB:1P6O, ECO:0007744|PDB:1RB7, ECO:0007744|PDB:1UAQ, ECO:0007744|PDB:1YSB, ECO:0007744|PDB:1YSD |
| Chain | Residue | Details |
| A | HIS62 | |
| A | CYS91 | |
| A | CYS94 | |
| B | HIS262 | |
| B | CYS291 | |
| B | CYS294 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1uaq |
| Chain | Residue | Details |
| A | GLU64 | |
| A | CYS91 | |
| A | SER89 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1uaq |
| Chain | Residue | Details |
| B | GLU264 | |
| B | CYS291 | |
| B | SER289 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 636 |
| Chain | Residue | Details |
| A | HIS62 | metal ligand |
| A | GLU64 | proton acceptor, proton donor |
| A | SER89 | electrostatic stabiliser |
| A | CYS91 | metal ligand |
| A | CYS94 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 636 |
| Chain | Residue | Details |
| B | HIS262 | metal ligand |
| B | GLU264 | proton acceptor, proton donor |
| B | SER289 | electrostatic stabiliser |
| B | CYS291 | metal ligand |
| B | CYS294 | metal ligand |
