1S1F
Crystal Structure of Streptomyces Coelicolor A3(2) CYP158A2 from antibiotic biosynthetic pathways
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| A | 0020037 | molecular_function | heme binding |
| A | 0042440 | biological_process | pigment metabolic process |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE HG A 435 |
| Chain | Residue |
| A | HIS287 |
| A | HEM430 |
| A | PIM431 |
| A | MLA433 |
| A | HOH523 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE HG A 436 |
| Chain | Residue |
| A | ILE154 |
| A | ILE157 |
| A | CYS158 |
| A | GLN240 |
| site_id | AC3 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE HEM A 430 |
| Chain | Residue |
| A | ARG71 |
| A | GLY94 |
| A | HIS101 |
| A | ARG105 |
| A | PHE112 |
| A | LEU239 |
| A | GLY242 |
| A | GLY243 |
| A | ASN249 |
| A | HIS287 |
| A | ARG295 |
| A | TYR318 |
| A | SER345 |
| A | PHE346 |
| A | HIS351 |
| A | CYS353 |
| A | PRO354 |
| A | GLY355 |
| A | ALA359 |
| A | PIM431 |
| A | MLA433 |
| A | HG435 |
| A | HOH445 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PIM A 431 |
| Chain | Residue |
| A | ILE87 |
| A | GLY242 |
| A | ALA245 |
| A | HEM430 |
| A | MLA432 |
| A | HG435 |
| A | HOH450 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MLA A 432 |
| Chain | Residue |
| A | PHE86 |
| A | ILE87 |
| A | PRO88 |
| A | ARG288 |
| A | GLY292 |
| A | LEU393 |
| A | PIM431 |
| A | HOH454 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE MLA A 433 |
| Chain | Residue |
| A | ARG288 |
| A | VAL291 |
| A | GLY292 |
| A | LEU293 |
| A | VAL316 |
| A | HEM430 |
| A | HG435 |
| A | HOH444 |
| A | HOH476 |
| A | HOH593 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 434 |
| Chain | Residue |
| A | ASP129 |
| A | ALA369 |
| A | ASP372 |
| A | ARG373 |
| A | HOH452 |
| A | HOH570 |
Functional Information from PROSITE/UniProt
| site_id | PS00086 |
| Number of Residues | 10 |
| Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGfGPHYCPG |
| Chain | Residue | Details |
| A | PHE346-GLY355 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15659395","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16239228","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1T93","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2D09","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"15659395","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16239228","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22203090","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1S1F","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SE6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1T93","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2D09","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2D0E","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3TZO","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Site: {"description":"Involved in determining product regiospecificity","evidences":[{"source":"PubMed","id":"22203090","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
