2IJ7
Structure of Mycobacterium tuberculosis CYP121 in complex with the antifungal drug fluconazole
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 | 0009975 | molecular_function | cyclase activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| A | 0016717 | molecular_function | oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water |
| A | 0020037 | molecular_function | heme binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070025 | molecular_function | carbon monoxide binding |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0009975 | molecular_function | cyclase activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| B | 0016717 | molecular_function | oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water |
| B | 0020037 | molecular_function | heme binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0070025 | molecular_function | carbon monoxide binding |
| C | 0004497 | molecular_function | monooxygenase activity |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0009975 | molecular_function | cyclase activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| C | 0016717 | molecular_function | oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water |
| C | 0020037 | molecular_function | heme binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0070025 | molecular_function | carbon monoxide binding |
| D | 0004497 | molecular_function | monooxygenase activity |
| D | 0005506 | molecular_function | iron ion binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0009975 | molecular_function | cyclase activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| D | 0016717 | molecular_function | oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water |
| D | 0020037 | molecular_function | heme binding |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0070025 | molecular_function | carbon monoxide binding |
| E | 0004497 | molecular_function | monooxygenase activity |
| E | 0005506 | molecular_function | iron ion binding |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0009975 | molecular_function | cyclase activity |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| E | 0016717 | molecular_function | oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water |
| E | 0020037 | molecular_function | heme binding |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0070025 | molecular_function | carbon monoxide binding |
| F | 0004497 | molecular_function | monooxygenase activity |
| F | 0005506 | molecular_function | iron ion binding |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0009975 | molecular_function | cyclase activity |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| F | 0016717 | molecular_function | oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water |
| F | 0020037 | molecular_function | heme binding |
| F | 0046872 | molecular_function | metal ion binding |
| F | 0070025 | molecular_function | carbon monoxide binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEM A 462 |
| Chain | Residue |
| A | MET62 |
| A | ARG286 |
| A | ALA337 |
| A | PHE338 |
| A | GLY339 |
| A | HIS343 |
| A | CYS345 |
| A | PRO346 |
| A | TPF2472 |
| A | HOH2527 |
| A | HOH2583 |
| A | MET86 |
| A | HOH2661 |
| A | HOH2792 |
| A | HIS146 |
| A | PHE230 |
| A | GLY234 |
| A | SER237 |
| A | PHE241 |
| A | PHE280 |
| A | LEU284 |
| site_id | AC2 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE HEM B 462 |
| Chain | Residue |
| B | MET62 |
| B | MET86 |
| B | HIS146 |
| B | PHE230 |
| B | GLY234 |
| B | SER237 |
| B | PHE280 |
| B | LEU284 |
| B | ARG286 |
| B | ALA337 |
| B | PHE338 |
| B | GLY339 |
| B | HIS343 |
| B | CYS345 |
| B | PRO346 |
| B | GLY347 |
| B | TPF2470 |
| B | HOH2517 |
| B | HOH2531 |
| B | HOH2547 |
| B | HOH2581 |
| B | HOH2631 |
| B | HOH2834 |
| site_id | AC3 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE HEM C 462 |
| Chain | Residue |
| C | MET62 |
| C | MET86 |
| C | HIS146 |
| C | PHE230 |
| C | GLY234 |
| C | SER237 |
| C | PHE241 |
| C | PHE280 |
| C | LEU284 |
| C | ARG286 |
| C | ALA337 |
| C | PHE338 |
| C | GLY339 |
| C | HIS343 |
| C | CYS345 |
| C | PRO346 |
| C | GLY347 |
| C | TPF2471 |
| C | HOH2477 |
| C | HOH2494 |
| C | HOH2516 |
| C | HOH2522 |
| C | HOH2598 |
| C | HOH2701 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEM D 462 |
| Chain | Residue |
| D | MET62 |
| D | MET86 |
| D | HIS146 |
| D | PHE230 |
| D | GLY234 |
| D | SER237 |
| D | PHE241 |
| D | PHE280 |
| D | LEU284 |
| D | ARG286 |
| D | ALA337 |
| D | PHE338 |
| D | GLY339 |
| D | GLN342 |
| D | HIS343 |
| D | CYS345 |
| D | PRO346 |
| D | TPF2473 |
| D | HOH2601 |
| D | HOH2623 |
| D | HOH2658 |
| D | HOH2748 |
| site_id | AC5 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE HEM E 462 |
| Chain | Residue |
| E | ARG286 |
| E | ALA337 |
| E | PHE338 |
| E | GLY339 |
| E | HIS343 |
| E | CYS345 |
| E | PRO346 |
| E | HOH481 |
| E | HOH483 |
| E | HOH615 |
| E | HOH849 |
| E | MET62 |
| E | MET86 |
| E | ARG95 |
| E | HIS146 |
| E | PHE230 |
| E | GLY234 |
| E | SER237 |
| E | PHE280 |
| E | LEU284 |
| site_id | AC6 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEM F 462 |
| Chain | Residue |
| F | MET62 |
| F | MET86 |
| F | HIS146 |
| F | PHE230 |
| F | GLY234 |
| F | SER237 |
| F | THR238 |
| F | PHE280 |
| F | LEU284 |
| F | ARG286 |
| F | ALA337 |
| F | PHE338 |
| F | GLY339 |
| F | HIS343 |
| F | CYS345 |
| F | PRO346 |
| F | TPF2474 |
| F | HOH2520 |
| F | HOH2617 |
| F | HOH2620 |
| F | HOH2648 |
| F | HOH2764 |
| site_id | AC7 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE TPF B 2470 |
| Chain | Residue |
| B | THR77 |
| B | VAL82 |
| B | VAL83 |
| B | ASN85 |
| B | MET86 |
| B | ALA167 |
| B | PHE168 |
| B | THR229 |
| B | GLN385 |
| B | HEM462 |
| B | HOH2547 |
| B | HOH2654 |
| B | HOH2677 |
| B | HOH2834 |
| site_id | AC8 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE TPF C 2471 |
| Chain | Residue |
| C | THR77 |
| C | VAL83 |
| C | ASN85 |
| C | MET86 |
| C | ALA167 |
| C | PHE168 |
| C | GLN385 |
| C | ARG386 |
| C | HEM462 |
| C | HOH2494 |
| C | HOH2516 |
| C | HOH2522 |
| C | HOH2624 |
| C | HOH2692 |
| site_id | AC9 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE TPF A 2472 |
| Chain | Residue |
| A | THR77 |
| A | VAL83 |
| A | ASN85 |
| A | MET86 |
| A | ALA167 |
| A | PHE168 |
| A | THR229 |
| A | ALA233 |
| A | SER237 |
| A | PHE280 |
| A | GLN385 |
| A | ARG386 |
| A | HEM462 |
| A | HOH2509 |
| A | HOH2519 |
| A | HOH2553 |
| A | HOH2583 |
| A | HOH2661 |
| A | HOH2761 |
| A | HOH2762 |
| A | HOH2792 |
| site_id | BC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE TPF D 2473 |
| Chain | Residue |
| D | THR77 |
| D | VAL83 |
| D | ASN85 |
| D | MET86 |
| D | ALA167 |
| D | PHE168 |
| D | THR229 |
| D | ALA233 |
| D | SER237 |
| D | GLN385 |
| D | ARG386 |
| D | HEM462 |
| D | HOH2516 |
| D | HOH2601 |
| D | HOH2652 |
| D | HOH2658 |
| D | HOH2667 |
| D | HOH2748 |
| site_id | BC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE TPF F 2474 |
| Chain | Residue |
| F | THR77 |
| F | VAL83 |
| F | ASN85 |
| F | MET86 |
| F | ALA167 |
| F | PHE168 |
| F | THR229 |
| F | ALA233 |
| F | SER237 |
| F | PHE280 |
| F | GLN385 |
| F | ARG386 |
| F | HEM462 |
| F | HOH2570 |
| F | HOH2575 |
| F | HOH2617 |
| F | HOH2764 |
Functional Information from PROSITE/UniProt
| site_id | PS00086 |
| Number of Residues | 10 |
| Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGrGQHFCPG |
| Chain | Residue | Details |
| A | PHE338-GLY347 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17028183","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19416919","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12435731","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17028183","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18818197","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19416919","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22890978","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23620594","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"description":"axial binding residue"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 12 |
| Details | Site: {"description":"Participates in a stacking interactions with the tyrosyl of cYY"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | Site: {"description":"Important for the position of heme"} |
| Chain | Residue | Details |
