6DGS
Crystal Structure of Leishmania major dihydroorotate dehydrogenase mutant Y142A
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004152 | molecular_function | dihydroorotate dehydrogenase activity |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006106 | biological_process | fumarate metabolic process |
| 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 | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| A | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
| A | 0097014 | cellular_component | ciliary plasm |
| A | 1990663 | molecular_function | dihydroorotate dehydrogenase (fumarate) activity |
| B | 0004152 | molecular_function | dihydroorotate dehydrogenase activity |
| B | 0005654 | cellular_component | nucleoplasm |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006106 | biological_process | fumarate metabolic process |
| 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 | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| B | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
| B | 0097014 | cellular_component | ciliary plasm |
| B | 1990663 | molecular_function | dihydroorotate dehydrogenase (fumarate) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | binding site for residue FMN A 401 |
| Chain | Residue |
| A | ALA19 |
| A | LYS165 |
| A | ILE194 |
| A | ASN195 |
| A | SER196 |
| A | GLY222 |
| A | GLY223 |
| A | VAL226 |
| A | CYS249 |
| A | GLY250 |
| A | GLY251 |
| A | ALA20 |
| A | GLY272 |
| A | THR273 |
| A | HOH525 |
| A | HOH535 |
| A | HOH542 |
| A | HOH592 |
| A | GLY21 |
| A | VAL22 |
| A | LYS44 |
| A | SER45 |
| A | ASN68 |
| A | MET70 |
| A | ASN128 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 402 |
| Chain | Residue |
| A | VAL202 |
| A | ILE203 |
| A | SO4403 |
| A | HOH511 |
| B | LEU227 |
| B | LEU231 |
| B | HOH573 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 A 403 |
| Chain | Residue |
| A | PRO63 |
| A | VAL202 |
| A | ILE203 |
| A | ASP204 |
| A | ARG298 |
| A | GOL402 |
| A | HOH590 |
| site_id | AC4 |
| Number of Residues | 24 |
| Details | binding site for residue FMN B 401 |
| Chain | Residue |
| B | ALA19 |
| B | ALA20 |
| B | GLY21 |
| B | LYS44 |
| B | SER45 |
| B | ASN68 |
| B | MET70 |
| B | ASN128 |
| B | LYS165 |
| B | ILE194 |
| B | ASN195 |
| B | SER196 |
| B | GLY222 |
| B | GLY223 |
| B | VAL226 |
| B | CYS249 |
| B | GLY250 |
| B | GLY251 |
| B | GLY272 |
| B | THR273 |
| B | HOH507 |
| B | HOH511 |
| B | HOH542 |
| B | HOH600 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue GOL B 402 |
| Chain | Residue |
| A | LEU227 |
| A | LEU231 |
| B | VAL202 |
| B | ILE203 |
| B | SO4403 |
| B | HOH517 |
| B | HOH580 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 B 403 |
| Chain | Residue |
| B | LEU62 |
| B | PRO63 |
| B | ASP204 |
| B | VAL211 |
| B | ARG298 |
| B | GOL402 |
