2FPT
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 | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 400 |
| Chain | Residue |
| A | ARG245 |
| A | VAL247 |
| A | HIS248 |
| A | HOH429 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ACT A 401 |
| Chain | Residue |
| A | ARG318 |
| A | HOH440 |
| A | LYS307 |
| A | PRO308 |
| A | ASP311 |
| A | THR314 |
| A | GLN315 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 402 |
| Chain | Residue |
| A | GLN165 |
| A | PRO204 |
| A | LEU205 |
| A | HIS248 |
| A | ARG298 |
| A | SER299 |
| A | HOH476 |
| A | HOH566 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 403 |
| Chain | Residue |
| A | HIS86 |
| A | ARG246 |
| A | VAL247 |
| A | ARG249 |
| A | HOH628 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 404 |
| Chain | Residue |
| A | ALA219 |
| A | GLY220 |
| A | ARG222 |
| A | HOH519 |
| A | HOH524 |
| A | HOH565 |
| A | HOH630 |
| site_id | AC6 |
| Number of Residues | 26 |
| 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 | LEU309 |
| A | VAL333 |
| A | GLY334 |
| A | GLY335 |
| A | LEU355 |
| A | TYR356 |
| A | THR357 |
| A | ORO399 |
| A | HOH407 |
| A | HOH428 |
| site_id | AC7 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ORO A 399 |
| Chain | Residue |
| A | LYS100 |
| A | ASN145 |
| A | TYR147 |
| A | GLY148 |
| A | PHE149 |
| A | ASN212 |
| A | SER215 |
| A | ASN217 |
| A | ASN284 |
| A | THR285 |
| A | FMN398 |
| site_id | AC8 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE ILB A 405 |
| Chain | Residue |
| A | TYR38 |
| A | LEU42 |
| A | LEU46 |
| A | GLN47 |
| A | ALA55 |
| A | HIS56 |
| A | ALA59 |
| A | PHE62 |
| A | LEU67 |
| A | LEU68 |
| A | PHE98 |
| A | VAL134 |
| A | ARG136 |
| A | TYR356 |
| A | LEU359 |
| A | THR360 |
| A | PRO364 |
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 | THR32-ARG396 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: Nucleophile |
| Chain | Residue | Details |
| A | SER215 |
| site_id | SWS_FT_FI3 |
| 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_FI4 |
| Number of Residues | 3 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | LYS100 | |
| A | ASN145 | |
| A | ASN284 |
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 | 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 |
