6OC0
Crystal structure of human DHODH with OSU-03012
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004151 | molecular_function | dihydroorotase activity |
| A | 0004152 | molecular_function | dihydroorotate dehydrogenase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005743 | cellular_component | mitochondrial inner membrane |
| A | 0005829 | cellular_component | cytosol |
| A | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
| A | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
| A | 0006225 | biological_process | UDP biosynthetic process |
| A | 0009220 | biological_process | pyrimidine ribonucleotide biosynthetic process |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | binding site for residue ORO A 401 |
| Chain | Residue |
| A | LYS99 |
| A | ASN283 |
| A | THR284 |
| A | FMN402 |
| A | ASN144 |
| A | TYR146 |
| A | GLY147 |
| A | PHE148 |
| A | ASN211 |
| A | SER214 |
| A | PRO215 |
| A | ASN216 |
| site_id | AC2 |
| Number of Residues | 25 |
| Details | binding site for residue FMN A 402 |
| Chain | Residue |
| A | ALA94 |
| A | ALA95 |
| A | GLY96 |
| A | LYS99 |
| A | SER119 |
| A | ASN144 |
| A | TYR146 |
| A | ASN180 |
| A | ASN211 |
| A | LYS254 |
| A | THR282 |
| A | ASN283 |
| A | THR284 |
| A | SER304 |
| A | GLY305 |
| A | LEU308 |
| A | VAL332 |
| A | GLY333 |
| A | GLY334 |
| A | LEU354 |
| A | TYR355 |
| A | THR356 |
| A | ORO401 |
| A | HOH529 |
| A | HOH545 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 403 |
| Chain | Residue |
| A | ARG244 |
| A | HIS247 |
| A | HOH708 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 404 |
| Chain | Residue |
| A | ARG56 |
| A | HIS100 |
| A | ASN149 |
| A | HIS151 |
| A | HOH600 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 405 |
| Chain | Residue |
| A | ARG245 |
| A | ARG248 |
| A | HOH721 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue M4J A 406 |
| Chain | Residue |
| A | TYR37 |
| A | PHE61 |
| A | THR62 |
| A | LEU66 |
| A | LEU67 |
| A | ARG69 |
| A | LEU358 |
| A | PRO363 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 364 |
| Details | TOPO_DOM: Mitochondrial intermembrane => ECO:0000250 |
| Chain | Residue | Details |
| A | THR31-ARG395 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: Nucleophile |
| Chain | Residue | Details |
| A | SER214 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 9 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10673429, ECO:0000269|PubMed:16480261 |
| Chain | Residue | Details |
| A | SER119 | |
| A | ASN180 | |
| A | ASN211 | |
| A | LYS254 | |
| A | THR282 | |
| A | GLY305 | |
| A | GLY334 | |
| A | TYR355 | |
| A | ALA95 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASN144 | |
| A | ASN283 | |
| A | LYS99 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 109 |
| Chain | Residue | Details |
| A | ASN144 | electrostatic stabiliser |
| A | PHE148 | activator, electrostatic stabiliser, enhance reactivity, polar/non-polar interaction |
| A | SER214 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, polar/non-polar interaction, proton acceptor, proton donor, proton relay |
| A | ASN216 | electrostatic stabiliser |
| A | THR217 | activator, electrostatic stabiliser, enhance reactivity, hydrogen bond acceptor |
| A | LYS254 | electrostatic stabiliser, hydrogen bond donor |
| A | ASN283 | electrostatic stabiliser |
