4OQV
High resolution crystal structure of human dihydroorotate dehydrogenase bound with DSM338 (N-[3,5-difluoro-4-(trifluoromethyl)phenyl]-5-methyl-2-(trifluoromethyl)[1,2,4]triazolo[1,5-a]pyrimidin-7-amine)
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 | 0005886 | cellular_component | plasma membrane |
| 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 501 |
| 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 | ORO502 |
| A | HOH603 |
| A | HOH608 |
| A | GLY97 |
| A | LYS100 |
| A | GLY119 |
| A | SER120 |
| A | ASN145 |
| A | TYR147 |
| A | ASN181 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ORO A 502 |
| Chain | Residue |
| A | LYS100 |
| A | ASN145 |
| A | TYR147 |
| A | GLY148 |
| A | PHE149 |
| A | ASN212 |
| A | ASN284 |
| A | THR285 |
| A | FMN501 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE 2V6 A 503 |
| Chain | Residue |
| A | MET43 |
| A | LEU46 |
| A | GLN47 |
| A | PRO52 |
| A | ALA55 |
| A | ALA59 |
| A | LEU68 |
| A | VAL134 |
| A | ARG136 |
| A | VAL143 |
| A | TYR356 |
| A | LEU359 |
| A | THR360 |
| A | PRO364 |
| A | HOH675 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACY A 504 |
| Chain | Residue |
| A | ALA169 |
| A | THR172 |
| A | LEU205 |
| A | ALA206 |
| A | ASP207 |
| A | HOH642 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACY A 505 |
| Chain | Residue |
| A | LYS307 |
| A | THR314 |
| A | GLN315 |
| A | ARG318 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 506 |
| Chain | Residue |
| A | PRO123 |
| A | SER155 |
| A | GLU197 |
| A | HOH821 |
| A | HOH955 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA A 507 |
| Chain | Residue |
| A | GLN166 |
| A | HIS248 |
| A | NA509 |
| A | HOH650 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 508 |
| Chain | Residue |
| A | ARG245 |
| A | VAL247 |
| A | HIS248 |
| A | NA509 |
| A | HOH826 |
| A | HOH900 |
| A | HOH933 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA A 509 |
| Chain | Residue |
| A | GLN166 |
| A | HIS248 |
| A | NA507 |
| A | SO4508 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Nucleophile |
| Chain | Residue | Details |
| A | SER215 |
| site_id | SWS_FT_FI2 |
| 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_FI3 |
| 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 |
