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 | ACT_SITE: Nucleophile |
Chain | Residue | Details |
A | SER175 | |
B | SER175 | |
D | SER175 | |
E | SER175 |
site_id | SWS_FT_FI2 |
Number of Residues | 32 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12220493 |
Chain | Residue | Details |
A | ALA62 | |
B | THR86 | |
B | ASN139 | |
B | LYS217 | |
B | THR245 | |
B | GLY268 | |
B | GLY297 | |
B | TYR318 | |
D | ALA62 | |
D | THR86 | |
D | ASN139 | |
A | THR86 | |
D | LYS217 | |
D | THR245 | |
D | GLY268 | |
D | GLY297 | |
D | TYR318 | |
E | ALA62 | |
E | THR86 | |
E | ASN139 | |
E | LYS217 | |
E | THR245 | |
A | ASN139 | |
E | GLY268 | |
E | GLY297 | |
E | TYR318 | |
A | LYS217 | |
A | THR245 | |
A | GLY268 | |
A | GLY297 | |
A | TYR318 | |
B | ALA62 |
site_id | SWS_FT_FI3 |
Number of Residues | 20 |
Details | BINDING: |
Chain | Residue | Details |
A | LYS66 | |
B | ASN246 | |
D | LYS66 | |
D | ASN111 | |
D | ASN172 | |
D | ASN177 | |
D | ASN246 | |
E | LYS66 | |
E | ASN111 | |
E | ASN172 | |
E | ASN177 | |
A | ASN111 | |
E | ASN246 | |
A | ASN172 | |
A | ASN177 | |
A | ASN246 | |
B | LYS66 | |
B | ASN111 | |
B | ASN172 | |
B | ASN177 |
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 |