6GEQ
Crystal structure of Mycobacterium tuberculosis cytochrome P450 CYP121A1 in complex with Triazole Pyrazole inhibitor 14a
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | binding site for residue HEM A 401 |
| Chain | Residue |
| A | MET62 |
| A | GLY339 |
| A | HIS343 |
| A | CYS345 |
| A | PRO346 |
| A | SO4403 |
| A | HOH512 |
| A | HOH527 |
| A | HOH590 |
| A | HOH595 |
| A | HOH722 |
| A | MET86 |
| A | HIS146 |
| A | GLY234 |
| A | SER237 |
| A | PHE280 |
| A | ARG286 |
| A | ALA337 |
| A | PHE338 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | binding site for residue EW5 A 402 |
| Chain | Residue |
| A | THR77 |
| A | VAL78 |
| A | VAL83 |
| A | ALA167 |
| A | PHE168 |
| A | VAL228 |
| A | THR229 |
| A | GLN385 |
| A | SO4403 |
| A | HOH673 |
| A | HOH716 |
| A | HOH734 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 403 |
| Chain | Residue |
| A | ARG386 |
| A | HEM401 |
| A | EW5402 |
| A | HOH512 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 A 404 |
| Chain | Residue |
| A | ARG58 |
| A | SER61 |
| A | MET62 |
| A | LYS63 |
| A | HIS343 |
| A | HOH518 |
| A | HOH588 |
| A | HOH613 |
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 | 4 |
| 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 | 1 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| 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 | 1 |
| Details | Binding site: {"description":"axial binding residue"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Site: {"description":"Participates in a stacking interactions with the tyrosyl of cYY"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Site: {"description":"Important for the position of heme"} |
| Chain | Residue | Details |
