1UUO
Rat dihydroorotate dehydrogenase (DHOD)in complex with brequinar
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004151 | molecular_function | dihydroorotase activity |
A | 0004152 | molecular_function | dihydroorotate dehydrogenase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0005739 | cellular_component | mitochondrion |
A | 0005743 | cellular_component | mitochondrial inner membrane |
A | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
A | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
A | 0006225 | biological_process | UDP biosynthetic process |
A | 0007565 | biological_process | female pregnancy |
A | 0007595 | biological_process | lactation |
A | 0009220 | biological_process | pyrimidine ribonucleotide biosynthetic process |
A | 0009410 | biological_process | response to xenobiotic stimulus |
A | 0010181 | molecular_function | FMN binding |
A | 0014070 | biological_process | response to organic cyclic compound |
A | 0016020 | cellular_component | membrane |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
A | 0031000 | biological_process | response to caffeine |
A | 0042594 | biological_process | response to starvation |
A | 0043025 | cellular_component | neuronal cell body |
A | 0043065 | biological_process | positive regulation of apoptotic process |
A | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
A | 0048038 | molecular_function | quinone binding |
A | 0048039 | molecular_function | ubiquinone binding |
A | 0090140 | biological_process | regulation of mitochondrial fission |
A | 0106430 | molecular_function | dihydroorotate dehydrogenase (quinone) activity |
A | 1903576 | biological_process | response to L-arginine |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NI A1400 |
Chain | Residue |
A | GLY203 |
A | PRO204 |
A | ALA206 |
A | THR247 |
A | ARG248 |
site_id | AC2 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE BRF A1397 |
Chain | Residue |
A | ALA55 |
A | HIS56 |
A | ALA59 |
A | VAL134 |
A | ARG136 |
A | TYR356 |
A | ILE360 |
A | PRO364 |
A | LEU42 |
A | MET43 |
A | GLN47 |
A | PRO52 |
site_id | AC3 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE FMN A1398 |
Chain | Residue |
A | ALA95 |
A | ALA96 |
A | GLY97 |
A | LYS100 |
A | GLY119 |
A | SER120 |
A | ASN145 |
A | ASN181 |
A | ASN212 |
A | LYS255 |
A | THR283 |
A | ASN284 |
A | SER305 |
A | GLY306 |
A | VAL333 |
A | GLY334 |
A | GLY335 |
A | LEU355 |
A | TYR356 |
A | THR357 |
A | ORO1399 |
A | HOH2025 |
A | HOH2034 |
A | HOH2041 |
site_id | AC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE ORO A1399 |
Chain | Residue |
A | LYS100 |
A | ASN145 |
A | TYR147 |
A | GLY148 |
A | PHE149 |
A | ASN212 |
A | SER215 |
A | ASN284 |
A | THR285 |
A | FMN1398 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 364 |
Details | TOPO_DOM: Mitochondrial matrix |
Chain | Residue | Details |
A | THR32-ARG396 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: Nucleophile => ECO:0000250 |
Chain | Residue | Details |
A | SER215 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15044733 |
Chain | Residue | Details |
A | ALA96 | |
A | SER120 | |
A | ASN181 | |
A | LYS255 | |
A | THR283 | |
A | GLY306 | |
A | GLY335 | |
A | TYR356 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: |
Chain | Residue | Details |
A | LYS100 | |
A | ASN145 | |
A | ASN212 | |
A | ASN284 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1h7x |
Chain | Residue | Details |
A | SER215 | |
A | PHE149 | |
A | LYS255 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1h7x |
Chain | Residue | Details |
A | SER215 |