1F76
ESCHERICHIA COLI DIHYDROOROTATE DEHYDROGENASE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004152 | molecular_function | dihydroorotate dehydrogenase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
| A | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
| A | 0006222 | biological_process | UMP biosynthetic process |
| A | 0009220 | biological_process | pyrimidine ribonucleotide biosynthetic process |
| A | 0010181 | molecular_function | FMN binding |
| 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 | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
| A | 0106430 | molecular_function | dihydroorotate dehydrogenase (quinone) activity |
| B | 0004152 | molecular_function | dihydroorotate dehydrogenase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
| B | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
| B | 0006222 | biological_process | UMP biosynthetic process |
| B | 0009220 | biological_process | pyrimidine ribonucleotide biosynthetic process |
| B | 0010181 | molecular_function | FMN binding |
| B | 0016020 | cellular_component | membrane |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| B | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
| B | 0106430 | molecular_function | dihydroorotate dehydrogenase (quinone) activity |
| D | 0004152 | molecular_function | dihydroorotate dehydrogenase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
| D | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
| D | 0006222 | biological_process | UMP biosynthetic process |
| D | 0009220 | biological_process | pyrimidine ribonucleotide biosynthetic process |
| D | 0010181 | molecular_function | FMN binding |
| D | 0016020 | cellular_component | membrane |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| D | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
| D | 0106430 | molecular_function | dihydroorotate dehydrogenase (quinone) activity |
| E | 0004152 | molecular_function | dihydroorotate dehydrogenase activity |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0005829 | cellular_component | cytosol |
| E | 0005886 | cellular_component | plasma membrane |
| E | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
| E | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
| E | 0006222 | biological_process | UMP biosynthetic process |
| E | 0009220 | biological_process | pyrimidine ribonucleotide biosynthetic process |
| E | 0010181 | molecular_function | FMN binding |
| E | 0016020 | cellular_component | membrane |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| E | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
| E | 0106430 | molecular_function | dihydroorotate dehydrogenase (quinone) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE FMN A 1337 |
| Chain | Residue |
| A | ALA61 |
| A | THR245 |
| A | THR247 |
| A | SER267 |
| A | GLY268 |
| A | LEU271 |
| A | VAL295 |
| A | GLY296 |
| A | GLY297 |
| A | TYR318 |
| A | SER319 |
| A | ALA62 |
| A | ORO1338 |
| A | HOH1352 |
| A | HOH1404 |
| A | HOH1675 |
| A | GLY63 |
| A | LYS66 |
| A | THR86 |
| A | ASN111 |
| A | ASN139 |
| A | ASN172 |
| A | LYS217 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ORO A 1338 |
| Chain | Residue |
| A | LYS66 |
| A | ASN111 |
| A | MSE113 |
| A | GLY114 |
| A | PHE115 |
| A | ASN172 |
| A | SER175 |
| A | ASN177 |
| A | ASN246 |
| A | THR247 |
| A | FMN1337 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ORO A 1339 |
| Chain | Residue |
| A | MSE1 |
| A | LEU37 |
| A | VAL38 |
| A | ARG39 |
| A | GLN40 |
| A | PRO326 |
| A | HOH1517 |
| A | HOH1528 |
| A | HOH1677 |
| site_id | AC4 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE FMN B 1437 |
| Chain | Residue |
| B | ALA61 |
| B | ALA62 |
| B | GLY63 |
| B | LYS66 |
| B | THR86 |
| B | ASN111 |
| B | ASN139 |
| B | ASN172 |
| B | LYS217 |
| B | THR245 |
| B | ASN246 |
| B | THR247 |
| B | SER267 |
| B | GLY268 |
| B | VAL295 |
| B | GLY296 |
| B | GLY297 |
| B | TYR318 |
| B | SER319 |
| B | FMT1439 |
| B | FMT1440 |
| B | HOH1441 |
| B | HOH1463 |
| site_id | AC5 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE FMN D 1537 |
| Chain | Residue |
| D | ALA61 |
| D | ALA62 |
| D | GLY63 |
| D | LYS66 |
| D | THR86 |
| D | ASN111 |
| D | ASN139 |
| D | ASN172 |
| D | LYS217 |
| D | THR245 |
| D | ASN246 |
| D | THR247 |
| D | SER267 |
| D | GLY268 |
| D | VAL295 |
| D | GLY296 |
| D | GLY297 |
| D | TYR318 |
| D | SER319 |
| D | FMT1538 |
| D | FMT1539 |
| D | HOH1542 |
| D | HOH1561 |
| D | HOH1564 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ORO D 1540 |
| Chain | Residue |
| D | MSE1 |
| D | LEU37 |
| D | VAL38 |
| D | GLN40 |
| D | PRO326 |
| D | HOH1617 |
| site_id | AC7 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE FMN E 1637 |
| Chain | Residue |
| E | LYS66 |
| E | THR86 |
| E | LEU100 |
| E | ASN111 |
| E | ASN139 |
| E | ASN172 |
| E | LYS217 |
| E | THR245 |
| E | ASN246 |
| E | THR247 |
| E | SER267 |
| E | GLY268 |
| E | LEU271 |
| E | VAL295 |
| E | GLY296 |
| E | GLY297 |
| E | TYR318 |
| E | SER319 |
| E | FMT1638 |
| E | FMT1640 |
| E | HOH1641 |
| E | HOH1653 |
| E | HOH1693 |
| E | ALA61 |
| E | ALA62 |
| E | GLY63 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT B 1438 |
| Chain | Residue |
| B | ASN111 |
| B | ASN177 |
| B | ASN246 |
| B | THR247 |
| B | FMT1439 |
| B | FMT1440 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FMT B 1439 |
| Chain | Residue |
| B | PHE115 |
| B | ASN172 |
| B | SER175 |
| B | ASN246 |
| B | FMN1437 |
| B | FMT1438 |
| B | FMT1440 |
| site_id | BC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FMT B 1440 |
| Chain | Residue |
| B | LYS66 |
| B | MSE113 |
| B | GLY114 |
| B | PHE115 |
| B | SER175 |
| B | ASN177 |
| B | FMN1437 |
| B | FMT1438 |
| B | FMT1439 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FMT D 1538 |
| Chain | Residue |
| D | ASN172 |
| D | SER175 |
| D | ASN246 |
| D | FMN1537 |
| D | FMT1539 |
| site_id | BC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FMT D 1539 |
| Chain | Residue |
| D | LYS66 |
| D | MSE113 |
| D | GLY114 |
| D | PHE115 |
| D | SER175 |
| D | ASN177 |
| D | FMN1537 |
| D | FMT1538 |
| D | HOH1557 |
| site_id | BC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FMT E 1638 |
| Chain | Residue |
| E | LYS66 |
| E | MSE113 |
| E | GLY114 |
| E | PHE115 |
| E | ASN177 |
| E | FMN1637 |
| E | FMT1639 |
| E | FMT1640 |
| site_id | BC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT E 1639 |
| Chain | Residue |
| E | ASN111 |
| E | ASN177 |
| E | THR247 |
| E | GLY265 |
| E | FMT1638 |
| E | FMT1640 |
| site_id | BC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FMT E 1640 |
| Chain | Residue |
| E | ASN172 |
| E | SER175 |
| E | PRO176 |
| E | ASN246 |
| E | FMN1637 |
| E | FMT1638 |
| E | FMT1639 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Nucleophile"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 40 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12220493","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | Binding site: {} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1h7x |
| Chain | Residue | Details |
| A | SER175 | |
| A | THR178 | |
| A | PHE115 | |
| A | LYS217 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1h7x |
| Chain | Residue | Details |
| B | SER175 | |
| B | THR178 | |
| B | PHE115 | |
| B | LYS217 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1h7x |
| Chain | Residue | Details |
| D | SER175 | |
| D | THR178 | |
| D | PHE115 | |
| D | LYS217 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1h7x |
| Chain | Residue | Details |
| E | SER175 | |
| E | THR178 | |
| E | PHE115 | |
| E | LYS217 |
| site_id | CSA5 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1h7x |
| Chain | Residue | Details |
| A | SER175 |
| site_id | CSA6 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1h7x |
| Chain | Residue | Details |
| B | SER175 |
| site_id | CSA7 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1h7x |
| Chain | Residue | Details |
| D | SER175 |
| site_id | CSA8 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1h7x |
| Chain | Residue | Details |
| E | SER175 |






