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 |
| B | 0004152 | molecular_function | dihydroorotate dehydrogenase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
| B | 0016020 | cellular_component | membrane |
| B | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | binding site for residue XCM A 1001 |
| Chain | Residue |
| A | PHE171 |
| A | GLY226 |
| A | ILE263 |
| A | ARG265 |
| A | TYR528 |
| A | LEU531 |
| A | VAL532 |
| A | GLY535 |
| A | FMN1002 |
| A | HOH1216 |
| A | LEU172 |
| A | CYS175 |
| A | GLY181 |
| A | GLU182 |
| A | CYS184 |
| A | HIS185 |
| A | PHE188 |
| A | LEU191 |
| 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 | CYS276 |
| A | ASN342 |
| A | LYS429 |
| A | SER457 |
| A | SER477 |
| A | GLY478 |
| A | SER505 |
| A | GLY506 |
| A | GLY507 |
| A | TYR528 |
| A | SER529 |
| A | XCM1001 |
| A | ORO1003 |
| A | HOH1112 |
| A | HOH1125 |
| A | HOH1127 |
| A | HOH1165 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | binding site for residue ORO A 1003 |
| Chain | Residue |
| A | LYS229 |
| A | ASN274 |
| A | CYS276 |
| A | GLY277 |
| A | PHE278 |
| A | ASN342 |
| A | SER345 |
| A | ASN347 |
| A | ASN458 |
| A | THR459 |
| A | FMN1002 |
| site_id | AC4 |
| Number of Residues | 18 |
| Details | binding site for residue XCM B 1001 |
| Chain | Residue |
| B | PHE171 |
| B | LEU172 |
| B | CYS175 |
| B | GLY181 |
| B | GLU182 |
| B | CYS184 |
| B | HIS185 |
| B | PHE188 |
| B | LEU191 |
| B | GLY226 |
| B | ILE263 |
| B | ARG265 |
| B | TYR528 |
| B | LEU531 |
| B | VAL532 |
| B | GLY535 |
| B | MET536 |
| B | HOH1195 |
| site_id | AC5 |
| Number of Residues | 22 |
| Details | binding site for residue FMN B 1002 |
| Chain | Residue |
| B | ALA224 |
| B | ALA225 |
| B | GLY226 |
| B | LYS229 |
| B | THR249 |
| B | ASN274 |
| B | ASN342 |
| B | LYS429 |
| B | SER457 |
| B | ASN458 |
| B | SER477 |
| B | GLY478 |
| B | SER505 |
| B | GLY506 |
| B | GLY507 |
| B | TYR528 |
| B | SER529 |
| B | ORO1003 |
| B | HOH1124 |
| B | HOH1132 |
| B | HOH1175 |
| B | HOH1190 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | binding site for residue ORO B 1003 |
| Chain | Residue |
| B | ASN347 |
| B | ASN458 |
| B | THR459 |
| B | FMN1002 |
| B | LYS229 |
| B | ASN274 |
| B | CYS276 |
| B | GLY277 |
| B | PHE278 |
| B | ASN342 |
| B | SER345 |
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 | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000250 |
| Chain | Residue | Details |
| A | SER345 | |
| B | SER345 | |
| Chain | Residue | Details |
| A | ALA225 | |
| B | GLY507 | |
| B | GLY535 | |
| B | LEU558 | |
| A | THR249 | |
| A | THR459 | |
| A | GLY507 | |
| A | GLY535 | |
| A | LEU558 | |
| B | ALA225 | |
| B | THR249 | |
| B | THR459 | |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | LYS229 | |
| B | PHE488 | |
| A | ASN274 | |
| A | ASN342 | |
| A | ASN347 | |
| A | PHE488 | |
| B | LYS229 | |
| B | ASN274 | |
| B | ASN342 | |
| B | ASN347 | |
