6L0B
Crystal structure of dihydroorotase in complex with fluorouracil from Saccharomyces cerevisiae
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004151 | molecular_function | dihydroorotase activity |
A | 0005634 | cellular_component | nucleus |
A | 0005737 | cellular_component | cytoplasm |
A | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
A | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
A | 0008270 | molecular_function | zinc ion binding |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016812 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides |
A | 0019856 | biological_process | pyrimidine nucleobase biosynthetic process |
A | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
A | 0046872 | molecular_function | metal ion binding |
B | 0004151 | molecular_function | dihydroorotase activity |
B | 0005634 | cellular_component | nucleus |
B | 0005737 | cellular_component | cytoplasm |
B | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
B | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
B | 0008270 | molecular_function | zinc ion binding |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016812 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides |
B | 0019856 | biological_process | pyrimidine nucleobase biosynthetic process |
B | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
B | 0046872 | molecular_function | metal ion binding |
C | 0004151 | molecular_function | dihydroorotase activity |
C | 0005634 | cellular_component | nucleus |
C | 0005737 | cellular_component | cytoplasm |
C | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
C | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
C | 0008270 | molecular_function | zinc ion binding |
C | 0016787 | molecular_function | hydrolase activity |
C | 0016812 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides |
C | 0019856 | biological_process | pyrimidine nucleobase biosynthetic process |
C | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
C | 0046872 | molecular_function | metal ion binding |
D | 0004151 | molecular_function | dihydroorotase activity |
D | 0005634 | cellular_component | nucleus |
D | 0005737 | cellular_component | cytoplasm |
D | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
D | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
D | 0008270 | molecular_function | zinc ion binding |
D | 0016787 | molecular_function | hydrolase activity |
D | 0016812 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides |
D | 0019856 | biological_process | pyrimidine nucleobase biosynthetic process |
D | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue ZN A 401 |
Chain | Residue |
A | HIS14 |
A | HIS16 |
A | KCX98 |
A | ASP258 |
A | ZN402 |
A | URF403 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue ZN A 402 |
Chain | Residue |
A | ZN401 |
A | URF403 |
A | KCX98 |
A | HIS137 |
A | HIS180 |
site_id | AC3 |
Number of Residues | 11 |
Details | binding site for residue URF A 403 |
Chain | Residue |
A | HIS16 |
A | ARG18 |
A | ASN43 |
A | THR105 |
A | THR106 |
A | ASP258 |
A | ALA260 |
A | HIS262 |
A | ALA275 |
A | ZN401 |
A | ZN402 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue ZN C 401 |
Chain | Residue |
C | KCX98 |
C | HIS137 |
C | HIS180 |
C | ZN402 |
C | URF403 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue ZN C 402 |
Chain | Residue |
C | HIS14 |
C | HIS16 |
C | KCX98 |
C | ASP258 |
C | ZN401 |
C | URF403 |
site_id | AC6 |
Number of Residues | 13 |
Details | binding site for residue URF C 403 |
Chain | Residue |
C | HIS16 |
C | ARG18 |
C | ASN43 |
C | KCX98 |
C | THR105 |
C | THR106 |
C | ASP258 |
C | ALA260 |
C | HIS262 |
C | ALA275 |
C | ZN401 |
C | ZN402 |
C | HOH503 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue ZN B 401 |
Chain | Residue |
B | HIS14 |
B | HIS16 |
B | KCX98 |
B | ASP258 |
B | ZN402 |
B | URF403 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue ZN B 402 |
Chain | Residue |
B | KCX98 |
B | HIS137 |
B | HIS180 |
B | ZN401 |
B | URF403 |
site_id | AC9 |
Number of Residues | 15 |
Details | binding site for residue URF B 403 |
Chain | Residue |
B | HIS16 |
B | ARG18 |
B | ASN43 |
B | KCX98 |
B | THR105 |
B | THR106 |
B | HIS137 |
B | HIS180 |
B | LYS230 |
B | ASP258 |
B | HIS262 |
B | ALA275 |
B | ZN401 |
B | ZN402 |
B | HOH535 |
site_id | AD1 |
Number of Residues | 5 |
Details | binding site for residue ZN D 401 |
Chain | Residue |
D | KCX98 |
D | HIS137 |
D | HIS180 |
D | ZN402 |
D | URF403 |
site_id | AD2 |
Number of Residues | 6 |
Details | binding site for residue ZN D 402 |
Chain | Residue |
D | HIS14 |
D | HIS16 |
D | KCX98 |
D | ASP258 |
D | ZN401 |
D | URF403 |
site_id | AD3 |
Number of Residues | 14 |
Details | binding site for residue URF D 403 |
Chain | Residue |
D | HIS16 |
D | ARG18 |
D | ASN43 |
D | KCX98 |
D | THR105 |
D | THR106 |
D | LYS230 |
D | ASP258 |
D | ALA260 |
D | HIS262 |
D | ALA275 |
D | GLY276 |
D | ZN401 |
D | ZN402 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 20 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P05020 |
Chain | Residue | Details |
A | HIS14 | |
C | ASP258 | |
B | HIS14 | |
B | HIS16 | |
B | HIS137 | |
B | HIS180 | |
B | ASP258 | |
D | HIS14 | |
D | HIS16 | |
D | HIS137 | |
D | HIS180 | |
A | HIS16 | |
D | ASP258 | |
A | HIS137 | |
A | HIS180 | |
A | ASP258 | |
C | HIS14 | |
C | HIS16 | |
C | HIS137 | |
C | HIS180 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: via carbamate group => ECO:0000250|UniProtKB:P05020 |
Chain | Residue | Details |
A | KCX98 | |
C | KCX98 | |
B | KCX98 | |
D | KCX98 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | MOD_RES: N6-carboxylysine => ECO:0000250|UniProtKB:P05020 |
Chain | Residue | Details |
A | KCX98 | |
C | KCX98 | |
B | KCX98 | |
D | KCX98 |