1P6O
The crystal structure of yeast cytosine deaminase bound to 4(R)-hydroxyl-3,4-dihydropyrimidine at 1.14 angstroms.
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 | 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 | 0034654 | biological_process | nucleobase-containing compound biosynthetic 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 | 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 | 0034654 | biological_process | nucleobase-containing compound biosynthetic 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 | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 400 |
Chain | Residue |
B | HIS262 |
B | CYS291 |
B | CYS294 |
B | HPY410 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 401 |
Chain | Residue |
A | HIS62 |
A | CYS91 |
A | CYS94 |
A | HPY411 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA B 402 |
Chain | Residue |
B | GLU328 |
B | GLN350 |
B | HOH1016 |
B | HOH1060 |
B | HOH1237 |
A | GLU75 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA B 403 |
Chain | Residue |
A | GLN150 |
A | HOH1231 |
A | HOH1311 |
B | GLU275 |
B | HOH1312 |
B | HOH1392 |
site_id | AC5 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE HPY B 410 |
Chain | Residue |
B | ILE233 |
B | ASN251 |
B | HIS262 |
B | GLY263 |
B | GLU264 |
B | PRO290 |
B | CYS291 |
B | CYS294 |
B | ASP355 |
B | ZN400 |
site_id | AC6 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE HPY A 411 |
Chain | Residue |
A | ILE33 |
A | ASN51 |
A | HIS62 |
A | GLY63 |
A | GLU64 |
A | PRO90 |
A | CYS91 |
A | CYS94 |
A | ASP155 |
A | ZN401 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACY A 420 |
Chain | Residue |
A | ASP42 |
A | HOH1214 |
A | HOH1222 |
A | HOH1228 |
B | ARG273 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ACY B 421 |
Chain | Residue |
B | GLY302 |
B | GLY326 |
B | HIS327 |
B | PHE353 |
B | HOH1093 |
B | HOH1188 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ACY B 422 |
Chain | Residue |
A | LYS77 |
B | ASN240 |
B | ASP281 |
B | PRO304 |
B | PHE353 |
B | HOH1105 |
B | HOH1162 |
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 |