Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004152 | molecular_function | dihydroorotate dehydrogenase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
| A | 0016020 | cellular_component | membrane |
| A | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE D65 A 1001 |
| Chain | Residue |
| A | LEU172 |
| A | LEU240 |
| A | ILE263 |
| A | ARG265 |
| A | ILE272 |
| A | LEU531 |
| A | MET536 |
| A | LEU176 |
| A | GLY181 |
| A | GLU182 |
| A | CYS184 |
| A | HIS185 |
| A | PHE188 |
| A | LEU197 |
| A | PHE227 |
| site_id | AC2 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE FMN A 1002 |
| Chain | Residue |
| A | ALA224 |
| A | ALA225 |
| A | GLY226 |
| A | LYS229 |
| A | THR249 |
| A | ASN274 |
| A | ASN342 |
| A | LYS429 |
| A | SER457 |
| A | ASN458 |
| A | SER477 |
| A | GLY478 |
| A | SER505 |
| A | GLY506 |
| A | GLY507 |
| A | TYR528 |
| A | SER529 |
| A | ORO1003 |
| A | HOH1105 |
| A | HOH1106 |
| A | HOH1107 |
| A | HOH1118 |
| A | HOH1156 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ORO A 1003 |
| Chain | Residue |
| A | LYS229 |
| A | ASN274 |
| A | CYS276 |
| A | GLY277 |
| A | PHE278 |
| A | ASN342 |
| A | SER344 |
| A | ASN458 |
| A | THR459 |
| A | FMN1002 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 1004 |
| Chain | Residue |
| A | GLU164 |
| A | ASN195 |
| A | ILE196 |
| A | LEU197 |
Functional Information from PROSITE/UniProt
| site_id | PS00911 |
| Number of Residues | 20 |
| Details | DHODEHASE_1 Dihydroorotate dehydrogenase signature 1. SfieiGTITprgQtGNakPR |
| Chain | Residue | Details |
| A | SER243-ARG262 | |
| site_id | PS00912 |
| Number of Residues | 21 |
| Details | DHODEHASE_2 Dihydroorotate dehydrogenase signature 2. IIAsGGIfSgldAleKIeAGA |
| Chain | Residue | Details |
| A | ILE502-ALA522 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16510978","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20702404","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 7 |
| Details | Binding site: {} |
