3ITQ
Crystal Structure of a Prolyl 4-Hydroxylase from Bacillus anthracis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004656 | molecular_function | procollagen-proline 4-dioxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| A | 0031418 | molecular_function | L-ascorbic acid binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051213 | molecular_function | dioxygenase activity |
| B | 0004656 | molecular_function | procollagen-proline 4-dioxygenase activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| B | 0031418 | molecular_function | L-ascorbic acid binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051213 | molecular_function | dioxygenase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 968 |
| Chain | Residue |
| A | TYR124 |
| A | HIS127 |
| A | ASP129 |
| A | HIS193 |
| A | TRP209 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 A 217 |
| Chain | Residue |
| B | HIS169 |
| A | LYS35 |
| A | GLU37 |
| B | GLU158 |
| B | SER167 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 B 218 |
| Chain | Residue |
| A | GLU158 |
| A | SER167 |
| A | HIS169 |
| B | LYS35 |
| B | GLU37 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 969 |
| Chain | Residue |
| B | TYR124 |
| B | HIS127 |
| B | ASP129 |
| B | VAL147 |
| B | PHE178 |
| B | HIS193 |
