3U2O
Dihydroorotate Dehydrogenase (DHODH) crystal structure in complex with small molecule inhibitor
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 | 26 |
Details | BINDING SITE FOR RESIDUE FMN A 500 |
Chain | Residue |
A | ALA95 |
A | ASN212 |
A | LYS255 |
A | THR283 |
A | ASN284 |
A | THR285 |
A | SER305 |
A | GLY306 |
A | LEU309 |
A | VAL333 |
A | GLY334 |
A | ALA96 |
A | GLY335 |
A | LEU355 |
A | TYR356 |
A | THR357 |
A | HOH402 |
A | ORO501 |
A | HOH512 |
A | GLY97 |
A | LYS100 |
A | GLY119 |
A | SER120 |
A | ASN145 |
A | TYR147 |
A | ASN181 |
site_id | AC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE ORO A 501 |
Chain | Residue |
A | LYS100 |
A | ASN145 |
A | TYR147 |
A | GLY148 |
A | PHE149 |
A | ASN212 |
A | SER215 |
A | ASN217 |
A | ASN284 |
A | THR285 |
A | FMN500 |
site_id | AC3 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE 03U A 1 |
Chain | Residue |
A | TYR38 |
A | MET43 |
A | LEU46 |
A | PRO52 |
A | HIS56 |
A | ALA59 |
A | PHE62 |
A | LEU68 |
A | PHE98 |
A | MET111 |
A | ARG136 |
A | TYR356 |
A | THR360 |
A | PRO364 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE ACT A 397 |
Chain | Residue |
A | LYS307 |
A | PRO308 |
A | ASP311 |
A | THR314 |
A | GLN315 |
A | ARG318 |
A | HOH410 |
A | HOH420 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ACT A 398 |
Chain | Residue |
A | LYS100 |
A | HIS101 |
A | TYR147 |
A | ASN150 |
A | HOH434 |
A | HOH611 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 400 |
Chain | Residue |
A | GLY220 |
A | ARG222 |
A | HOH594 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 401 |
Chain | Residue |
A | ARG245 |
A | VAL247 |
A | HIS248 |
A | HOH566 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 9 |
Details | TOPO_DOM: Mitochondrial matrix => ECO:0000250 |
Chain | Residue | Details |
A | MET2-ALA11 |
site_id | SWS_FT_FI2 |
Number of Residues | 19 |
Details | TRANSMEM: Helical => ECO:0000250 |
Chain | Residue | Details |
A | GLN12-ALA31 |
site_id | SWS_FT_FI3 |
Number of Residues | 364 |
Details | TOPO_DOM: Mitochondrial intermembrane => ECO:0000250 |
Chain | Residue | Details |
A | THR32-ARG396 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | ACT_SITE: Nucleophile |
Chain | Residue | Details |
A | SER215 |
site_id | SWS_FT_FI5 |
Number of Residues | 9 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10673429, ECO:0000269|PubMed:16480261 |
Chain | Residue | Details |
A | ALA96 | |
A | SER120 | |
A | ASN181 | |
A | ASN212 | |
A | LYS255 | |
A | THR283 | |
A | GLY306 | |
A | GLY335 | |
A | TYR356 |
site_id | SWS_FT_FI6 |
Number of Residues | 3 |
Details | BINDING: |
Chain | Residue | Details |
A | LYS100 | |
A | ASN145 | |
A | ASN284 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 7 |
Details | M-CSA 109 |
Chain | Residue | Details |
A | ASN145 | electrostatic stabiliser |
A | PHE149 | activator, electrostatic stabiliser, enhance reactivity, polar/non-polar interaction |
A | SER215 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, polar/non-polar interaction, proton acceptor, proton donor, proton relay |
A | ASN217 | electrostatic stabiliser |
A | THR218 | activator, electrostatic stabiliser, enhance reactivity, hydrogen bond acceptor |
A | LYS255 | electrostatic stabiliser, hydrogen bond donor |
A | ASN284 | electrostatic stabiliser |