4IPW
Substrate and reaction specificity of Mycobacterium tuberculosis cytochrome P450 CYP121
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 | 23 |
| Details | BINDING SITE FOR RESIDUE HEM A 401 |
| Chain | Residue |
| A | MET62 |
| A | ARG286 |
| A | ALA337 |
| A | PHE338 |
| A | GLY339 |
| A | HIS343 |
| A | CYS345 |
| A | PRO346 |
| A | 1G7406 |
| A | HOH501 |
| A | HOH524 |
| A | MET86 |
| A | HOH567 |
| A | HOH613 |
| A | HOH722 |
| A | HOH1088 |
| A | HIS146 |
| A | PHE230 |
| A | GLY234 |
| A | SER237 |
| A | PHE241 |
| A | PHE280 |
| A | LEU284 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 A 402 |
| Chain | Residue |
| A | ARG58 |
| A | SER61 |
| A | MET62 |
| A | LYS63 |
| A | HIS343 |
| A | HOH784 |
| A | HOH793 |
| A | HOH834 |
| A | HOH1082 |
| A | HOH1107 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 403 |
| Chain | Residue |
| A | SER12 |
| A | ARG17 |
| A | HOH672 |
| A | HOH711 |
| A | HOH766 |
| A | HOH890 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 404 |
| Chain | Residue |
| A | LEU7 |
| A | ARG32 |
| A | ARG300 |
| A | HOH783 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 405 |
| Chain | Residue |
| A | ARG134 |
| A | ASN135 |
| A | PHE161 |
| A | ARG381 |
| A | ARG391 |
| A | HOH563 |
| A | HOH657 |
| site_id | AC6 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE 1G7 A 406 |
| Chain | Residue |
| A | MET62 |
| A | THR77 |
| A | VAL78 |
| A | VAL82 |
| A | VAL83 |
| A | ASN85 |
| A | ALA167 |
| A | PHE168 |
| A | THR229 |
| A | ARG386 |
| A | HEM401 |
| A | HOH502 |
| A | HOH540 |
| A | HOH546 |
| A | HOH567 |
| A | HOH623 |
| A | HOH751 |
| A | HOH865 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 407 |
| Chain | Residue |
| A | MET62 |
| A | THR65 |
| A | ARG72 |
| A | ASN74 |
| A | LEU76 |
| A | PRO285 |
| A | HOH566 |
| A | HOH751 |
| A | HOH972 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 408 |
| Chain | Residue |
| A | VAL5 |
| A | GLU64 |
| A | ALA67 |
| A | THR289 |
| A | LYS301 |
| A | HOH868 |
| A | HOH889 |
| A | HOH1026 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 409 |
| Chain | Residue |
| A | VAL5 |
| A | GLU8 |
| A | ALA68 |
| A | GLY69 |
| A | ALA70 |
| A | PRO71 |
| A | GLY302 |
| A | HOH1026 |
| site_id | BC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 A 410 |
| Chain | Residue |
| A | HOH760 |
| A | HOH761 |
| A | HOH902 |
| A | LYS211 |
| A | PRO330 |
| A | ASN331 |
| A | PRO332 |
| A | THR333 |
| A | SER334 |
| site_id | BC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL A 411 |
| Chain | Residue |
| A | GLU81 |
| A | TRP182 |
| A | ILE186 |
| A | GLU221 |
| A | THR225 |
| A | GLN254 |
| A | HOH573 |
| A | HOH625 |
| A | HOH626 |
| A | HOH875 |
| site_id | BC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 412 |
| Chain | Residue |
| A | ASP16 |
| A | SER248 |
| A | GLN251 |
| A | ARG252 |
| A | ILE276 |
| A | HOH560 |
| A | HOH764 |
| A | HOH1132 |
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 |
