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 | 0006707 | biological_process | cholesterol catabolic process |
A | 0008395 | molecular_function | steroid hydroxylase activity |
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 | 0036199 | molecular_function | cholest-4-en-3-one 26-monooxygenase activity |
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 | 0006707 | biological_process | cholesterol catabolic process |
B | 0008395 | molecular_function | steroid hydroxylase activity |
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 | 0036199 | molecular_function | cholest-4-en-3-one 26-monooxygenase activity |
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 | 0006707 | biological_process | cholesterol catabolic process |
C | 0008395 | molecular_function | steroid hydroxylase activity |
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 | 0036199 | molecular_function | cholest-4-en-3-one 26-monooxygenase activity |
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 | 0006707 | biological_process | cholesterol catabolic process |
D | 0008395 | molecular_function | steroid hydroxylase activity |
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 | 0036199 | molecular_function | cholest-4-en-3-one 26-monooxygenase activity |
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 | 0006707 | biological_process | cholesterol catabolic process |
E | 0008395 | molecular_function | steroid hydroxylase activity |
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 | 0036199 | molecular_function | cholest-4-en-3-one 26-monooxygenase activity |
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 | 0006707 | biological_process | cholesterol catabolic process |
F | 0008395 | molecular_function | steroid hydroxylase activity |
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 | 0036199 | molecular_function | cholest-4-en-3-one 26-monooxygenase activity |
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: BINDING => ECO:0000269|PubMed:17028183, ECO:0000269|PubMed:19416919 |
Chain | Residue | Details |
A | THR77 | |
C | SER237 | |
C | LYS301 | |
C | GLN385 | |
D | THR77 | |
D | SER237 | |
D | LYS301 | |
D | GLN385 | |
E | THR77 | |
E | SER237 | |
E | LYS301 | |
A | SER237 | |
E | GLN385 | |
F | THR77 | |
F | SER237 | |
F | LYS301 | |
F | GLN385 | |
A | LYS301 | |
A | GLN385 | |
B | THR77 | |
B | SER237 | |
B | LYS301 | |
B | GLN385 | |
C | THR77 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: |
Chain | Residue | Details |
A | ASN85 | |
B | ASN85 | |
C | ASN85 | |
D | ASN85 | |
E | ASN85 | |
F | ASN85 |
site_id | SWS_FT_FI3 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12435731, ECO:0000269|PubMed:17028183, ECO:0000269|PubMed:18818197, ECO:0000269|PubMed:19416919, ECO:0000269|PubMed:22890978, ECO:0000269|PubMed:23620594 |
Chain | Residue | Details |
A | ARG286 | |
E | HIS343 | |
F | ARG286 | |
F | HIS343 | |
A | HIS343 | |
B | ARG286 | |
B | HIS343 | |
C | ARG286 | |
C | HIS343 | |
D | ARG286 | |
D | HIS343 | |
E | ARG286 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | BINDING: axial binding residue |
Chain | Residue | Details |
A | CYS345 | |
B | CYS345 | |
C | CYS345 | |
D | CYS345 | |
E | CYS345 | |
F | CYS345 |
site_id | SWS_FT_FI5 |
Number of Residues | 12 |
Details | SITE: Participates in a stacking interactions with the tyrosyl of cYY |
Chain | Residue | Details |
A | PHE168 | |
E | TRP182 | |
F | PHE168 | |
F | TRP182 | |
A | TRP182 | |
B | PHE168 | |
B | TRP182 | |
C | PHE168 | |
C | TRP182 | |
D | PHE168 | |
D | TRP182 | |
E | PHE168 |
site_id | SWS_FT_FI6 |
Number of Residues | 6 |
Details | SITE: Important for the position of heme |
Chain | Residue | Details |
A | PRO346 | |
B | PRO346 | |
C | PRO346 | |
D | PRO346 | |
E | PRO346 | |
F | PRO346 |