6B8S
Crystal Structure of Dihydroorotate Dehydrogenase from Helicobacter pylori with bound FMN
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004152 | molecular_function | dihydroorotate dehydrogenase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0005886 | cellular_component | plasma membrane |
A | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
A | 0006221 | biological_process | pyrimidine nucleotide 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 |
B | 0004152 | molecular_function | dihydroorotate dehydrogenase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0005886 | cellular_component | plasma membrane |
B | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
B | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
B | 0016020 | cellular_component | membrane |
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 | 0106430 | molecular_function | dihydroorotate dehydrogenase (quinone) activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 22 |
Details | binding site for residue FMN A 401 |
Chain | Residue |
A | ALA66 |
A | THR242 |
A | ASN243 |
A | SER261 |
A | GLY262 |
A | LEU265 |
A | VAL289 |
A | GLY290 |
A | GLY291 |
A | ILE311 |
A | TYR312 |
A | ALA67 |
A | SER313 |
A | HOH505 |
A | HOH523 |
A | GLY68 |
A | LYS71 |
A | THR91 |
A | ASN116 |
A | ASN145 |
A | ASN178 |
A | LYS214 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue PGE A 402 |
Chain | Residue |
A | TYR3 |
A | HIS19 |
A | PHE315 |
A | ILE316 |
A | HOH526 |
site_id | AC3 |
Number of Residues | 20 |
Details | binding site for residue FMN B 401 |
Chain | Residue |
B | ALA66 |
B | ALA67 |
B | GLY68 |
B | THR91 |
B | ASN116 |
B | ASN145 |
B | ASN178 |
B | LYS214 |
B | THR242 |
B | ASN243 |
B | SER261 |
B | GLY262 |
B | LEU265 |
B | VAL289 |
B | GLY290 |
B | GLY291 |
B | TYR312 |
B | SER313 |
B | HOH508 |
B | HOH509 |
site_id | AC4 |
Number of Residues | 1 |
Details | binding site for residue PGE B 402 |
Chain | Residue |
B | SER32 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_00225 |
Chain | Residue | Details |
A | SER181 | |
B | SER181 |
site_id | SWS_FT_FI2 |
Number of Residues | 26 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00225 |
Chain | Residue | Details |
A | ALA67 | |
A | ASN243 | |
A | GLY262 | |
A | GLY291 | |
A | TYR312 | |
B | ALA67 | |
B | LYS71 | |
B | THR91 | |
B | ASN116 | |
B | ASN145 | |
B | ASN178 | |
A | LYS71 | |
B | ASN183 | |
B | LYS214 | |
B | THR242 | |
B | ASN243 | |
B | GLY262 | |
B | GLY291 | |
B | TYR312 | |
A | THR91 | |
A | ASN116 | |
A | ASN145 | |
A | ASN178 | |
A | ASN183 | |
A | LYS214 | |
A | THR242 |