4J25
Crystal structure of a Pseudomonas putida prolyl-4-hydroxylase (P4H)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0008198 | molecular_function | ferrous iron binding |
| 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 | 0031543 | molecular_function | peptidyl-proline dioxygenase activity |
| A | 0071456 | biological_process | cellular response to hypoxia |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0008198 | molecular_function | ferrous iron binding |
| 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 | 0031543 | molecular_function | peptidyl-proline dioxygenase activity |
| B | 0071456 | biological_process | cellular response to hypoxia |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0008198 | molecular_function | ferrous iron binding |
| 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 | 0031543 | molecular_function | peptidyl-proline dioxygenase activity |
| C | 0071456 | biological_process | cellular response to hypoxia |
| D | 0005506 | molecular_function | iron ion binding |
| D | 0008198 | molecular_function | ferrous iron binding |
| 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 | 0031543 | molecular_function | peptidyl-proline dioxygenase activity |
| D | 0071456 | biological_process | cellular response to hypoxia |
| E | 0005506 | molecular_function | iron ion binding |
| E | 0008198 | molecular_function | ferrous iron binding |
| E | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| E | 0031418 | molecular_function | L-ascorbic acid binding |
| E | 0031543 | molecular_function | peptidyl-proline dioxygenase activity |
| E | 0071456 | biological_process | cellular response to hypoxia |
| F | 0005506 | molecular_function | iron ion binding |
| F | 0008198 | molecular_function | ferrous iron binding |
| F | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| F | 0031418 | molecular_function | L-ascorbic acid binding |
| F | 0031543 | molecular_function | peptidyl-proline dioxygenase activity |
| F | 0071456 | biological_process | cellular response to hypoxia |
| G | 0005506 | molecular_function | iron ion binding |
| G | 0008198 | molecular_function | ferrous iron binding |
| G | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| G | 0031418 | molecular_function | L-ascorbic acid binding |
| G | 0031543 | molecular_function | peptidyl-proline dioxygenase activity |
| G | 0071456 | biological_process | cellular response to hypoxia |
| H | 0005506 | molecular_function | iron ion binding |
| H | 0008198 | molecular_function | ferrous iron binding |
| H | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| H | 0031418 | molecular_function | L-ascorbic acid binding |
| H | 0031543 | molecular_function | peptidyl-proline dioxygenase activity |
| H | 0071456 | biological_process | cellular response to hypoxia |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN A 401 |
| Chain | Residue |
| A | HIS124 |
| A | ASP126 |
| A | HIS183 |
| A | OGA402 |
| A | HOH503 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE OGA A 402 |
| Chain | Residue |
| A | LEU154 |
| A | HIS183 |
| A | VAL185 |
| A | ARG192 |
| A | THR196 |
| A | MN401 |
| A | HOH503 |
| A | HOH579 |
| A | TYR121 |
| A | HIS124 |
| A | ASP126 |
| A | TYR141 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN B 401 |
| Chain | Residue |
| B | HIS124 |
| B | ASP126 |
| B | HIS183 |
| B | OGA402 |
| B | HOH518 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE OGA B 402 |
| Chain | Residue |
| B | HIS124 |
| B | ASP126 |
| B | TYR141 |
| B | LEU154 |
| B | HIS183 |
| B | VAL185 |
| B | ARG192 |
| B | SER194 |
| B | THR196 |
| B | TRP198 |
| B | MN401 |
| B | HOH518 |
| B | HOH561 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN C 401 |
| Chain | Residue |
| C | HIS124 |
| C | ASP126 |
| C | HIS183 |
| C | OGA402 |
| C | HOH508 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE OGA C 402 |
| Chain | Residue |
| C | TYR121 |
| C | HIS124 |
| C | ASP126 |
| C | TYR141 |
| C | LEU154 |
| C | HIS183 |
| C | VAL185 |
| C | ARG192 |
| C | THR196 |
| C | TRP198 |
| C | MN401 |
| C | HOH508 |
| C | HOH536 |
| C | HOH575 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN D 401 |
| Chain | Residue |
| D | HIS124 |
| D | ASP126 |
| D | HIS183 |
| D | OGA402 |
| D | HOH505 |
| site_id | AC8 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE OGA D 402 |
| Chain | Residue |
| D | TYR121 |
| D | HIS124 |
| D | ASP126 |
| D | TYR141 |
| D | LEU154 |
| D | HIS183 |
| D | ARG192 |
| D | SER194 |
| D | THR196 |
| D | MN401 |
| D | HOH505 |
| D | HOH546 |
| D | HOH580 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN E 401 |
| Chain | Residue |
| E | HIS124 |
| E | ASP126 |
| E | HIS183 |
| E | OGA402 |
| E | HOH509 |
| site_id | BC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE OGA E 402 |
| Chain | Residue |
| E | TYR121 |
| E | HIS124 |
| E | ASP126 |
| E | TYR141 |
| E | HIS183 |
| E | VAL185 |
| E | ARG192 |
| E | SER194 |
| E | THR196 |
| E | TRP198 |
| E | MN401 |
| E | HOH504 |
| E | HOH507 |
| E | HOH509 |
| E | HOH524 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN F 401 |
| Chain | Residue |
| F | HIS124 |
| F | ASP126 |
| F | HIS183 |
| F | OGA402 |
| F | HOH506 |
| site_id | BC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE OGA F 402 |
| Chain | Residue |
| F | HIS124 |
| F | ASP126 |
| F | TYR141 |
| F | HIS183 |
| F | VAL185 |
| F | ARG192 |
| F | THR196 |
| F | MN401 |
| F | HOH506 |
| F | HOH508 |
| F | TYR115 |
| F | TYR121 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN G 401 |
| Chain | Residue |
| G | HIS124 |
| G | ASP126 |
| G | HIS183 |
| G | OGA402 |
| G | HOH505 |
| site_id | BC5 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE OGA G 402 |
| Chain | Residue |
| G | TYR115 |
| G | TYR121 |
| G | HIS124 |
| G | ASP126 |
| G | VAL139 |
| G | TYR141 |
| G | HIS183 |
| G | VAL185 |
| G | ARG192 |
| G | THR196 |
| G | TRP198 |
| G | MN401 |
| G | HOH505 |
| G | HOH509 |
| G | HOH539 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN H 401 |
| Chain | Residue |
| H | HIS124 |
| H | ASP126 |
| H | HIS183 |
| H | OGA402 |
| H | HOH502 |
| site_id | BC7 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE OGA H 402 |
| Chain | Residue |
| H | TYR115 |
| H | TYR121 |
| H | HIS124 |
| H | ASP126 |
| H | VAL139 |
| H | TYR141 |
| H | LEU154 |
| H | HIS183 |
| H | ARG192 |
| H | THR196 |
| H | TRP198 |
| H | MN401 |
| H | HOH502 |
| H | HOH507 |
| H | HOH528 |
