5V7Y
Prolyl 4-Hydroxylase Interacts with and Modifies Elongation Factor Tu
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 |
| C | 0004656 | molecular_function | procollagen-proline 4-dioxygenase activity |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| C | 0031418 | molecular_function | L-ascorbic acid binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051213 | molecular_function | dioxygenase activity |
| D | 0004656 | molecular_function | procollagen-proline 4-dioxygenase activity |
| D | 0005506 | molecular_function | iron ion binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| D | 0031418 | molecular_function | L-ascorbic acid binding |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0051213 | molecular_function | dioxygenase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue CO A 301 |
| Chain | Residue |
| A | HIS127 |
| A | ASP129 |
| A | HIS193 |
| A | IMD302 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | binding site for residue IMD A 302 |
| Chain | Residue |
| A | THR207 |
| A | TRP209 |
| A | CO301 |
| A | TFA303 |
| A | TYR124 |
| A | HIS127 |
| A | ASP129 |
| A | VAL147 |
| A | HIS193 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | binding site for residue TFA A 303 |
| Chain | Residue |
| A | TYR118 |
| A | TYR124 |
| A | VAL147 |
| A | THR159 |
| A | GLY194 |
| A | GLY195 |
| A | LYS203 |
| A | ILE205 |
| A | IMD302 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue CO B 301 |
| Chain | Residue |
| B | HIS127 |
| B | ASP129 |
| B | HIS193 |
| B | AKG302 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | binding site for residue AKG B 302 |
| Chain | Residue |
| B | TYR118 |
| B | TYR124 |
| B | HIS127 |
| B | ASP129 |
| B | THR159 |
| B | HIS193 |
| B | GLY195 |
| B | LYS203 |
| B | ILE205 |
| B | THR207 |
| B | TRP209 |
| B | CO301 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue CO D 301 |
| Chain | Residue |
| D | HIS127 |
| D | ASP129 |
| D | HIS193 |
| D | IMD302 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue IMD D 302 |
| Chain | Residue |
| D | TYR124 |
| D | HIS127 |
| D | ASP129 |
| D | HIS193 |
| D | THR207 |
| D | TRP209 |
| D | CO301 |
| D | TFA305 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue IMD D 303 |
| Chain | Residue |
| C | ARG212 |
| D | ASN104 |
| D | HOH493 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue IMD D 304 |
| Chain | Residue |
| A | ASP184 |
| D | TYR128 |
| D | PHE131 |
| D | HOH404 |
| D | HOH414 |
| site_id | AD1 |
| Number of Residues | 8 |
| Details | binding site for residue TFA D 305 |
| Chain | Residue |
| D | TYR118 |
| D | TYR124 |
| D | THR159 |
| D | GLY194 |
| D | GLY195 |
| D | LYS203 |
| D | ILE205 |
| D | IMD302 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue MPD D 306 |
| Chain | Residue |
| C | GLN13 |
| C | PHE181 |
| D | HIS109 |
| D | ARG212 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue CO C 301 |
| Chain | Residue |
| C | HIS127 |
| C | ASP129 |
| C | HIS193 |
| C | IMD302 |
| site_id | AD4 |
| Number of Residues | 7 |
| Details | binding site for residue IMD C 302 |
| Chain | Residue |
| C | HIS127 |
| C | ASP129 |
| C | VAL147 |
| C | HIS193 |
| C | THR207 |
| C | CO301 |
| C | TFA303 |
| site_id | AD5 |
| Number of Residues | 10 |
| Details | binding site for residue TFA C 303 |
| Chain | Residue |
| C | TYR118 |
| C | TYR124 |
| C | VAL147 |
| C | THR159 |
| C | HIS193 |
| C | GLY194 |
| C | GLY195 |
| C | LYS203 |
| C | ILE205 |
| C | IMD302 |
