1YSB
Yeast Cytosine Deaminase Triple Mutant
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 | 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 | 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 |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004131 | molecular_function | cytosine deaminase activity |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| 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 | 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 500 |
| Chain | Residue |
| B | HIS262 |
| B | CYS291 |
| B | CYS294 |
| B | ZN502 |
| B | HOH1332 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 501 |
| Chain | Residue |
| A | HOH1335 |
| A | HIS62 |
| A | CYS91 |
| A | CYS94 |
| A | ZN503 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN B 502 |
| Chain | Residue |
| B | GLU264 |
| B | ZN500 |
| B | HOH1054 |
| B | HOH1331 |
| B | HOH1332 |
| B | HOH1333 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 503 |
| Chain | Residue |
| A | GLU64 |
| A | ZN501 |
| A | HOH1044 |
| A | HOH1334 |
| A | HOH1335 |
| A | HOH1336 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 504 |
| Chain | Residue |
| B | GLY326 |
| B | ASP346 |
| B | HOH1026 |
| B | HOH1065 |
| B | HOH1071 |
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 | 240 |
| Details | Domain: {"description":"CMP/dCMP-type deaminase","evidences":[{"source":"PROSITE-ProRule","id":"PRU01083","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"12637534","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1UAQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12637534","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12906827","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1P6O","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1UAQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12637534","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12906827","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15879217","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1OX7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1P6O","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1RB7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1UAQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1YSB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1YSD","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
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 |
