3W1A
Structure of Trypanosoma cruzi dihydroorotate dehydrogenase in complex with 5-halogenated orotate derivatives
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004152 | molecular_function | dihydroorotate dehydrogenase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
| A | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
| A | 0006222 | biological_process | UMP biosynthetic process |
| 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 | 1990663 | molecular_function | dihydroorotate dehydrogenase (fumarate) activity |
| B | 0004152 | molecular_function | dihydroorotate dehydrogenase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
| B | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
| B | 0006222 | biological_process | UMP biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| B | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
| B | 1990663 | molecular_function | dihydroorotate dehydrogenase (fumarate) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE FMN A 401 |
| Chain | Residue |
| A | ALA18 |
| A | ASN194 |
| A | GLY221 |
| A | GLY222 |
| A | ILE225 |
| A | CYS248 |
| A | GLY249 |
| A | GLY250 |
| A | GLY271 |
| A | THR272 |
| A | FOT403 |
| A | ALA19 |
| A | HOH508 |
| A | HOH518 |
| A | HOH528 |
| A | HOH878 |
| A | GLY20 |
| A | LYS43 |
| A | SER44 |
| A | ASN67 |
| A | ASN127 |
| A | LYS164 |
| A | VAL193 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE NCO A 402 |
| Chain | Residue |
| A | GLN275 |
| A | GLU276 |
| A | GLY278 |
| A | HOH683 |
| A | HOH839 |
| A | HOH851 |
| B | GLN275 |
| B | GLU276 |
| B | GLY278 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE FOT A 403 |
| Chain | Residue |
| A | LYS43 |
| A | ASN67 |
| A | MET69 |
| A | GLY70 |
| A | LEU71 |
| A | ASN127 |
| A | CYS130 |
| A | PRO131 |
| A | ASN132 |
| A | ASN194 |
| A | SER195 |
| A | FMN401 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 404 |
| Chain | Residue |
| A | CYS31 |
| A | ALA34 |
| A | HOH532 |
| B | CYS31 |
| B | ALA34 |
| B | SER35 |
| B | HOH696 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 405 |
| Chain | Residue |
| A | LYS214 |
| A | GLN215 |
| A | PHE217 |
| A | HOH543 |
| A | HOH555 |
| A | HOH597 |
| A | HOH685 |
| B | ILE171 |
| B | ARG239 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 406 |
| Chain | Residue |
| A | THR176 |
| A | HOH554 |
| A | HOH813 |
| B | ARG112 |
| B | HOH587 |
| site_id | AC7 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE FMN B 401 |
| Chain | Residue |
| B | ALA18 |
| B | ALA19 |
| B | GLY20 |
| B | LYS43 |
| B | SER44 |
| B | ASN67 |
| B | ASN127 |
| B | LYS164 |
| B | VAL193 |
| B | ASN194 |
| B | GLY221 |
| B | GLY222 |
| B | ILE225 |
| B | CYS248 |
| B | GLY249 |
| B | GLY250 |
| B | GLY271 |
| B | THR272 |
| B | FOT402 |
| B | HOH506 |
| B | HOH518 |
| B | HOH524 |
| B | HOH862 |
| site_id | AC8 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE FOT B 402 |
| Chain | Residue |
| B | FMN401 |
| B | LYS43 |
| B | ASN67 |
| B | MET69 |
| B | GLY70 |
| B | LEU71 |
| B | ASN127 |
| B | CYS130 |
| B | PRO131 |
| B | ASN132 |
| B | ASN194 |
| B | SER195 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 403 |
| Chain | Residue |
| A | ILE171 |
| A | ARG239 |
| B | LYS214 |
| B | GLN215 |
| B | PHE217 |
| B | HOH604 |
| B | HOH831 |
| B | HOH860 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 404 |
| Chain | Residue |
| A | LEU80 |
| A | ARG112 |
| A | HOH529 |
| A | HOH567 |
| B | ASP175 |
| B | THR176 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 405 |
| Chain | Residue |
| B | LEU4 |
| B | ASN5 |
| B | ARG305 |
| B | HOH667 |
| B | HOH700 |
| B | HOH702 |
| B | HOH797 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18302934","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | Binding site: {} |
| Chain | Residue | Details |
