2FPV
Dual binding mode of a novel series of DHODH inhibitors
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 | 7 |
| Details | BINDING SITE FOR RESIDUE ACT A 400 |
| Chain | Residue |
| A | LYS307 |
| A | PRO308 |
| A | ASP311 |
| A | THR314 |
| A | GLN315 |
| A | ARG318 |
| A | HOH428 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT A 401 |
| Chain | Residue |
| A | THR172 |
| A | LEU205 |
| A | ASP207 |
| A | HOH440 |
| A | GLN168 |
| A | ALA169 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 402 |
| Chain | Residue |
| A | ARG245 |
| A | VAL247 |
| A | HIS248 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 403 |
| Chain | Residue |
| A | ARG246 |
| A | ARG249 |
| A | HOH629 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 404 |
| Chain | Residue |
| A | ARG160 |
| A | GLN325 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 406 |
| Chain | Residue |
| A | SER262 |
| A | LYS265 |
| A | ALA291 |
| A | GLY292 |
| A | GLU319 |
| A | HOH454 |
| A | HOH510 |
| A | HOH631 |
| site_id | AC7 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE FMN A 398 |
| Chain | Residue |
| A | ALA95 |
| A | ALA96 |
| A | GLY97 |
| A | LYS100 |
| A | GLY119 |
| A | SER120 |
| A | ASN145 |
| A | TYR147 |
| A | ASN181 |
| A | ASN212 |
| A | LYS255 |
| A | THR283 |
| A | ASN284 |
| A | THR285 |
| A | SER305 |
| A | GLY306 |
| A | VAL333 |
| A | GLY334 |
| A | GLY335 |
| A | LEU355 |
| A | TYR356 |
| A | THR357 |
| A | ORO399 |
| A | HOH409 |
| A | HOH415 |
| site_id | AC8 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ORO A 399 |
| Chain | Residue |
| A | LYS100 |
| A | ASN145 |
| A | ARG146 |
| A | TYR147 |
| A | GLY148 |
| A | PHE149 |
| A | ASN212 |
| A | SER215 |
| A | ASN217 |
| A | ASN284 |
| A | THR285 |
| A | FMN398 |
| site_id | AC9 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE ILC A 405 |
| Chain | Residue |
| A | TYR38 |
| A | LEU46 |
| A | GLN47 |
| A | ALA55 |
| A | HIS56 |
| A | ALA59 |
| A | THR63 |
| A | LEU67 |
| A | LEU68 |
| A | PHE98 |
| A | ARG136 |
| A | TYR356 |
| A | LEU359 |
| A | THR360 |
| A | PRO364 |
| A | HOH497 |
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 | ASN212 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 9 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10673429, ECO:0000269|PubMed:16480261 |
| Chain | Residue | Details |
| A | GLY93 | |
| A | GLU117 | |
| A | LEU178 | |
| A | LEU209 | |
| A | VAL252 | |
| A | LEU280 | |
| A | GLY303 | |
| A | GLY332 | |
| A | VAL353 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | GLY97 | |
| A | ALA142 | |
| A | ILE281 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1h7x |
| Chain | Residue | Details |
| A | SER215 | |
| A | THR218 | |
| A | PHE149 | |
| A | LYS255 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1h7x |
| Chain | Residue | Details |
| A | SER215 |
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 109 |
| Chain | Residue | Details |
| A | ALA142 | electrostatic stabiliser |
| A | ARG146 | activator, electrostatic stabiliser, enhance reactivity, polar/non-polar interaction |
| A | ASN212 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, polar/non-polar interaction, proton acceptor, proton donor, proton relay |
| A | SER214 | electrostatic stabiliser |
| A | SER215 | activator, electrostatic stabiliser, enhance reactivity, hydrogen bond acceptor |
| A | VAL252 | electrostatic stabiliser, hydrogen bond donor |
| A | ILE281 | electrostatic stabiliser |
