6DWG
Crystal structure of Leishmania major dihydroorotate dehydrogenase mutant Q139A
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
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 | 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 | 0097014 | cellular_component | ciliary plasm |
A | 1990663 | molecular_function | dihydroorotate dehydrogenase (fumarate) activity |
B | 0000166 | molecular_function | nucleotide binding |
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 | 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 | 0097014 | cellular_component | ciliary plasm |
B | 1990663 | molecular_function | dihydroorotate dehydrogenase (fumarate) activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 20 |
Details | binding site for residue FMN A 401 |
Chain | Residue |
A | ALA19 |
A | GLY222 |
A | GLY223 |
A | VAL226 |
A | CYS249 |
A | GLY250 |
A | GLY251 |
A | GLY272 |
A | THR273 |
A | HOH512 |
A | HOH542 |
A | ALA20 |
A | HOH557 |
A | GLY21 |
A | LYS44 |
A | SER45 |
A | ASN68 |
A | LYS165 |
A | ILE194 |
A | ASN195 |
site_id | AC2 |
Number of Residues | 2 |
Details | binding site for residue SO4 A 402 |
Chain | Residue |
A | ASP204 |
A | GOL405 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue SO4 A 403 |
Chain | Residue |
A | ARG239 |
A | THR311 |
A | HOH543 |
A | HOH605 |
site_id | AC4 |
Number of Residues | 2 |
Details | binding site for residue SO4 A 404 |
Chain | Residue |
A | HIS160 |
A | SER161 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue GOL A 405 |
Chain | Residue |
A | ILE203 |
A | SO4402 |
A | HOH504 |
A | HOH520 |
B | LEU231 |
site_id | AC6 |
Number of Residues | 2 |
Details | binding site for residue NI A 406 |
Chain | Residue |
A | HIS174 |
A | HOH640 |
site_id | AC7 |
Number of Residues | 21 |
Details | binding site for residue FMN B 401 |
Chain | Residue |
B | ALA19 |
B | ALA20 |
B | GLY21 |
B | LYS44 |
B | SER45 |
B | ASN68 |
B | ASN128 |
B | LYS165 |
B | ILE194 |
B | ASN195 |
B | GLY222 |
B | GLY223 |
B | VAL226 |
B | CYS249 |
B | GLY250 |
B | GLY251 |
B | GLY272 |
B | THR273 |
B | HOH508 |
B | HOH510 |
B | HOH593 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue GOL B 402 |
Chain | Residue |
A | LEU227 |
B | VAL202 |
B | ILE203 |
B | GOL404 |
B | HOH505 |
site_id | AC9 |
Number of Residues | 9 |
Details | binding site for residue GOL B 403 |
Chain | Residue |
A | PRO138 |
A | ASN199 |
A | LYS215 |
A | HOH552 |
B | ASP171 |
B | PHE172 |
B | ALA173 |
B | HOH622 |
B | HOH650 |
site_id | AD1 |
Number of Residues | 1 |
Details | binding site for residue GOL B 404 |
Chain | Residue |
B | GOL402 |