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 | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 1006 |
Chain | Residue |
A | LYS193 |
A | LYS193 |
A | LYS193 |
A | TYR194 |
A | TYR194 |
A | TYR194 |
site_id | AC2 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE A26 A 1001 |
Chain | Residue |
A | CYS184 |
A | HIS185 |
A | PHE188 |
A | ILE263 |
A | ARG265 |
A | TYR528 |
A | VAL532 |
A | GLY535 |
A | MET536 |
A | PHE171 |
A | LEU172 |
A | GLY181 |
site_id | AC3 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE FMN A 1002 |
Chain | Residue |
A | ALA224 |
A | ALA225 |
A | GLY226 |
A | LYS229 |
A | GLY248 |
A | THR249 |
A | ILE263 |
A | ILE272 |
A | ASN274 |
A | ASN342 |
A | LYS429 |
A | SER457 |
A | SER477 |
A | GLY478 |
A | LEU481 |
A | SER505 |
A | GLY506 |
A | GLY507 |
A | TYR528 |
A | SER529 |
A | ORO1003 |
A | HOH1009 |
A | HOH1011 |
A | HOH1014 |
A | HOH1031 |
site_id | AC4 |
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 | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE N8E A 1004 |
Chain | Residue |
A | ASP169 |
A | LEU172 |
A | LYS173 |
A | TYR551 |
A | GLY554 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE N8E A 1005 |
Chain | Residue |
A | ILE170 |
A | PHE171 |
A | PHE174 |
A | LEU187 |
A | ILE196 |
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 | ACT_SITE: Nucleophile => ECO:0000250 |
Chain | Residue | Details |
A | SER345 | |
Chain | Residue | Details |
A | ALA225 | |
A | THR249 | |
A | LYS429 | |
A | SER477 | |
A | SER505 | |
A | TYR528 | |
site_id | SWS_FT_FI3 |
Number of Residues | 5 |
Details | BINDING: |
Chain | Residue | Details |
A | LYS229 | |
A | ASN274 | |
A | ASN342 | |
A | ASN347 | |
A | ASN458 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1h7x |
Chain | Residue | Details |
A | THR348 | |
A | PHE278 | |
A | SER345 | |
A | LYS429 | |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1h7x |
Chain | Residue | Details |
A | SER345 | |