2WH8
Interaction of Mycobacterium tuberculosis CYP130 with heterocyclic arylamines
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0009274 | cellular_component | peptidoglycan-based cell wall |
| 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 |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0009274 | cellular_component | peptidoglycan-based cell wall |
| 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 |
| C | 0004497 | molecular_function | monooxygenase activity |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0009274 | cellular_component | peptidoglycan-based cell wall |
| 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 |
| D | 0004497 | molecular_function | monooxygenase activity |
| D | 0005506 | molecular_function | iron ion binding |
| D | 0009274 | cellular_component | peptidoglycan-based cell wall |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEM A 450 |
| Chain | Residue |
| A | LEU71 |
| A | LEU293 |
| A | ARG295 |
| A | TYR318 |
| A | THR346 |
| A | PHE347 |
| A | SER348 |
| A | ALA351 |
| A | HIS352 |
| A | CYS354 |
| A | GLY356 |
| A | MET89 |
| A | II2460 |
| A | HOH2045 |
| A | VAL90 |
| A | HIS97 |
| A | ARG101 |
| A | MET240 |
| A | GLY244 |
| A | THR247 |
| A | VAL248 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE II2 A 460 |
| Chain | Residue |
| A | LEU71 |
| A | PRO88 |
| A | VAL90 |
| A | MET91 |
| A | ALA235 |
| A | PHE238 |
| A | THR239 |
| A | THR242 |
| A | GLY243 |
| A | HEM450 |
| A | HOH2128 |
| A | HOH2207 |
| D | LEU187 |
| site_id | AC3 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE HEM B 450 |
| Chain | Residue |
| B | MET89 |
| B | VAL90 |
| B | HIS97 |
| B | ARG101 |
| B | MET240 |
| B | GLY244 |
| B | THR247 |
| B | LEU293 |
| B | ARG295 |
| B | TYR318 |
| B | THR346 |
| B | PHE347 |
| B | SER348 |
| B | HIS352 |
| B | CYS354 |
| B | GLY356 |
| B | II2460 |
| B | HOH2070 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE II2 B 460 |
| Chain | Residue |
| B | LEU71 |
| B | PRO88 |
| B | VAL90 |
| B | MET91 |
| B | PHE238 |
| B | THR239 |
| B | THR242 |
| B | GLY243 |
| B | HEM450 |
| B | HOH2144 |
| B | HOH2232 |
| C | LEU187 |
| site_id | AC5 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE HEM C 450 |
| Chain | Residue |
| C | MET89 |
| C | VAL90 |
| C | HIS97 |
| C | ARG101 |
| C | MET240 |
| C | GLY244 |
| C | THR247 |
| C | LEU293 |
| C | ARG295 |
| C | TYR318 |
| C | THR346 |
| C | PHE347 |
| C | SER348 |
| C | HIS352 |
| C | CYS354 |
| C | GLY356 |
| C | II2460 |
| C | HOH2033 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE II2 C 460 |
| Chain | Residue |
| B | LEU187 |
| C | LEU71 |
| C | PRO88 |
| C | VAL90 |
| C | MET91 |
| C | ALA235 |
| C | PHE238 |
| C | THR239 |
| C | THR242 |
| C | GLY243 |
| C | HEM450 |
| C | HOH2169 |
| site_id | AC7 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE HEM D 450 |
| Chain | Residue |
| D | GLY244 |
| D | THR247 |
| D | LEU293 |
| D | ARG295 |
| D | TYR318 |
| D | THR346 |
| D | PHE347 |
| D | SER348 |
| D | HIS352 |
| D | CYS354 |
| D | GLY356 |
| D | II2460 |
| D | HOH2065 |
| D | MET89 |
| D | VAL90 |
| D | HIS97 |
| D | ARG101 |
| D | MET240 |
| site_id | AC8 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE II2 D 460 |
| Chain | Residue |
| A | LEU187 |
| D | LEU71 |
| D | PRO88 |
| D | VAL90 |
| D | MET91 |
| D | ALA235 |
| D | PHE238 |
| D | THR239 |
| D | THR242 |
| D | GLY243 |
| D | HEM450 |
| D | HOH2144 |
Functional Information from PROSITE/UniProt
| site_id | PS00086 |
| Number of Residues | 10 |
| Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FShGAHHCLG |
| Chain | Residue | Details |
| A | PHE347-GLY356 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASP93 | |
| A | HIS97 | |
| B | ASP93 | |
| B | HIS97 | |
| C | ASP93 | |
| C | HIS97 | |
| D | ASP93 | |
| D | HIS97 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18089574, ECO:0000269|PubMed:19605350 |
| Chain | Residue | Details |
| A | ARG101 | |
| B | TYR318 | |
| B | SER348 | |
| B | HIS352 | |
| C | ARG101 | |
| C | GLY243 | |
| C | ARG295 | |
| C | TYR318 | |
| C | SER348 | |
| C | HIS352 | |
| D | ARG101 | |
| A | GLY243 | |
| D | GLY243 | |
| D | ARG295 | |
| D | TYR318 | |
| D | SER348 | |
| D | HIS352 | |
| A | ARG295 | |
| A | TYR318 | |
| A | SER348 | |
| A | HIS352 | |
| B | ARG101 | |
| B | GLY243 | |
| B | ARG295 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: axial binding residue |
| Chain | Residue | Details |
| A | CYS354 | |
| B | CYS354 | |
| C | CYS354 | |
| D | CYS354 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1akd |
| Chain | Residue | Details |
| A | ASP246 | |
| A | THR247 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1akd |
| Chain | Residue | Details |
| B | ASP246 | |
| B | THR247 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1akd |
| Chain | Residue | Details |
| C | ASP246 | |
| C | THR247 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1akd |
| Chain | Residue | Details |
| D | ASP246 | |
| D | THR247 |
