3A4Z
Structure of cytochrome P450 Vdh mutant (Vdh-K1) obtained by directed evolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| A | 0020037 | molecular_function | heme binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047748 | molecular_function | cholestanetetraol 26-dehydrogenase activity |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| B | 0020037 | molecular_function | heme binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0047748 | molecular_function | cholestanetetraol 26-dehydrogenase activity |
| C | 0004497 | molecular_function | monooxygenase activity |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| C | 0020037 | molecular_function | heme binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0047748 | molecular_function | cholestanetetraol 26-dehydrogenase activity |
| D | 0004497 | molecular_function | monooxygenase activity |
| D | 0005506 | molecular_function | iron ion binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| D | 0020037 | molecular_function | heme binding |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0047748 | molecular_function | cholestanetetraol 26-dehydrogenase activity |
| E | 0004497 | molecular_function | monooxygenase activity |
| E | 0005506 | molecular_function | iron ion binding |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| E | 0020037 | molecular_function | heme binding |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0047748 | molecular_function | cholestanetetraol 26-dehydrogenase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEM A 412 |
| Chain | Residue |
| A | PHE58 |
| A | VAL283 |
| A | PRO287 |
| A | ARG289 |
| A | LEU312 |
| A | PHE339 |
| A | PHE340 |
| A | GLY341 |
| A | ILE344 |
| A | HIS345 |
| A | CYS347 |
| A | LYS65 |
| A | GLY349 |
| A | ALA353 |
| A | HOH425 |
| A | ILE88 |
| A | HIS95 |
| A | ARG99 |
| A | PHE106 |
| A | ALA236 |
| A | THR240 |
| A | THR241 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 2501 |
| Chain | Residue |
| A | ASP204 |
| A | HOH580 |
| A | HOH582 |
| A | HOH601 |
| A | HOH768 |
| A | GOL3002 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 2505 |
| Chain | Residue |
| A | GLY128 |
| A | HOH610 |
| A | HOH690 |
| A | HOH795 |
| A | HOH796 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CA A 2506 |
| Chain | Residue |
| A | ASP320 |
| D | ASP320 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT A 4006 |
| Chain | Residue |
| A | HIS342 |
| A | GLY343 |
| A | PHE346 |
| A | HOH573 |
| A | HOH594 |
| A | HOH613 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 3001 |
| Chain | Residue |
| A | ASP53 |
| A | GLU56 |
| A | HOH427 |
| A | HOH558 |
| D | ARG55 |
| D | HOH462 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 3002 |
| Chain | Residue |
| A | ASP204 |
| A | HOH552 |
| A | HOH768 |
| A | CA2501 |
| E | ARG70 |
| E | PRO72 |
| E | ALA304 |
| site_id | AC8 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEM B 412 |
| Chain | Residue |
| B | PHE58 |
| B | LYS65 |
| B | ILE88 |
| B | HIS95 |
| B | ARG99 |
| B | PHE106 |
| B | ALA236 |
| B | THR240 |
| B | THR241 |
| B | VAL283 |
| B | PRO287 |
| B | ARG289 |
| B | LEU312 |
| B | PHE339 |
| B | PHE340 |
| B | GLY341 |
| B | ILE344 |
| B | HIS345 |
| B | CYS347 |
| B | ALA353 |
| B | HOH419 |
| site_id | AC9 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEM C 412 |
| Chain | Residue |
| C | PHE58 |
| C | LYS65 |
| C | MET87 |
| C | ILE88 |
| C | HIS95 |
| C | ARG99 |
| C | PHE106 |
| C | LEU233 |
| C | ALA236 |
| C | THR240 |
| C | THR241 |
| C | ARG289 |
| C | LEU312 |
| C | PHE339 |
| C | PHE340 |
| C | GLY341 |
| C | ILE344 |
| C | HIS345 |
| C | CYS347 |
| C | GLY349 |
| C | ALA353 |
| C | HOH433 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA C 2503 |
| Chain | Residue |
| C | HOH429 |
| C | HOH436 |
| C | HOH466 |
| C | ACT4004 |
| C | ASP204 |
| C | HOH428 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT C 4004 |
| Chain | Residue |
| A | ARG70 |
| A | PRO72 |
| C | ASP204 |
| C | HOH428 |
| C | HOH477 |
| C | CA2503 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT C 4007 |
| Chain | Residue |
| C | HIS342 |
| C | GLY343 |
| C | PHE346 |
| C | HOH489 |
| site_id | BC4 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEM D 412 |
| Chain | Residue |
| D | PHE58 |
| D | LYS65 |
| D | ILE88 |
| D | HIS95 |
| D | ARG99 |
| D | PHE106 |
| D | LEU232 |
| D | ALA236 |
| D | THR240 |
| D | THR241 |
| D | VAL283 |
| D | PRO287 |
| D | ARG289 |
| D | LEU312 |
| D | PHE339 |
| D | PHE340 |
| D | GLY341 |
| D | HIS345 |
| D | CYS347 |
| D | ALA353 |
| D | HOH446 |
| site_id | BC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CA D 2502 |
| Chain | Residue |
| B | HOH649 |
| D | ASP204 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT D 4001 |
| Chain | Residue |
| D | HIS342 |
| D | GLY343 |
| D | PHE346 |
| D | HOH454 |
| D | HOH485 |
| site_id | BC7 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEM E 412 |
| Chain | Residue |
| E | PHE58 |
| E | LYS65 |
| E | MET87 |
| E | ILE88 |
| E | HIS95 |
| E | ARG99 |
| E | PHE106 |
| E | ALA236 |
| E | THR240 |
| E | THR241 |
| E | VAL283 |
| E | PRO287 |
| E | ARG289 |
| E | LEU312 |
| E | PHE339 |
| E | PHE340 |
| E | GLY341 |
| E | HIS345 |
| E | CYS347 |
| E | LEU348 |
| E | ALA353 |
| E | HOH438 |
| site_id | BC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA E 2504 |
| Chain | Residue |
| C | HOH423 |
| E | ASP204 |
| E | HOH458 |
| E | HOH792 |
| E | ACT4005 |
| site_id | BC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT E 4005 |
| Chain | Residue |
| C | ARG70 |
| E | ASP204 |
| E | HOH747 |
| E | CA2504 |
| site_id | CC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT E 4008 |
| Chain | Residue |
| E | HIS342 |
| E | GLY343 |
| E | PHE346 |
Functional Information from PROSITE/UniProt
| site_id | PS00086 |
| Number of Residues | 10 |
| Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGhGIHFCLG |
| Chain | Residue | Details |
| A | PHE340-GLY349 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 5 |
| Details | BINDING: axial binding residue => ECO:0000250|UniProtKB:P0A512 |
| Chain | Residue | Details |
| A | CYS347 | |
| B | CYS347 | |
| C | CYS347 | |
| D | CYS347 | |
| E | CYS347 |
