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 | 20 |
Details | binding site for residue XCV A 1001 |
Chain | Residue |
A | PHE171 |
A | LEU191 |
A | GLY226 |
A | LYS229 |
A | ILE263 |
A | ARG265 |
A | TYR528 |
A | LEU531 |
A | VAL532 |
A | GLY535 |
A | HOH1157 |
A | LEU172 |
A | HOH1239 |
A | CYS175 |
A | GLY181 |
A | GLU182 |
A | CYS184 |
A | HIS185 |
A | LEU187 |
A | PHE188 |
site_id | AC2 |
Number of Residues | 22 |
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 | HOH1114 |
A | HOH1124 |
A | HOH1141 |
A | HOH1224 |
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 | 20 |
Details | binding site for residue XCV 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 | LYS229 |
B | ILE263 |
B | ARG265 |
B | TYR528 |
B | LEU531 |
B | VAL532 |
B | GLY535 |
B | HOH1110 |
B | HOH1143 |
B | HOH1219 |
site_id | AC5 |
Number of Residues | 23 |
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 | LEU481 |
B | SER505 |
B | GLY506 |
B | GLY507 |
B | TYR528 |
B | SER529 |
B | ORO1003 |
B | HOH1111 |
B | HOH1126 |
B | HOH1149 |
B | HOH1154 |
site_id | AC6 |
Number of Residues | 11 |
Details | binding site for residue ORO B 1003 |
Chain | Residue |
B | GLY277 |
B | PHE278 |
B | ASN342 |
B | SER345 |
B | ASN347 |
B | ASN458 |
B | THR459 |
B | FMN1002 |
B | LYS229 |
B | ASN274 |
B | CYS276 |
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 | |