1SE6
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 |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| B | 0020037 | molecular_function | heme binding |
| B | 0042440 | biological_process | pigment metabolic process |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SPK A 631 |
| Chain | Residue |
| A | GLY376 |
| A | LYS378 |
| A | ALA380 |
| A | HIS405 |
| B | LYS378 |
| B | THR403 |
| site_id | AC2 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE HEM A 430 |
| Chain | Residue |
| A | HIS101 |
| A | ARG105 |
| A | LEU239 |
| A | GLY242 |
| A | ALA245 |
| A | LEU282 |
| A | HIS287 |
| A | ARG295 |
| A | TYR318 |
| A | SER345 |
| A | PHE346 |
| A | HIS351 |
| A | CYS353 |
| A | PRO354 |
| A | ALA359 |
| A | HOH694 |
| A | HOH771 |
| A | ARG71 |
| A | VAL93 |
| A | GLY94 |
| site_id | AC3 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEM B 430 |
| Chain | Residue |
| B | ARG71 |
| B | VAL93 |
| B | GLY94 |
| B | HIS101 |
| B | ARG105 |
| B | PHE112 |
| B | LEU239 |
| B | GLY242 |
| B | ALA245 |
| B | ASN249 |
| B | HIS287 |
| B | ARG295 |
| B | TYR318 |
| B | SER345 |
| B | PHE346 |
| B | HIS351 |
| B | CYS353 |
| B | PRO354 |
| B | HOH445 |
| B | HOH495 |
| B | HOH534 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MES A 632 |
| Chain | Residue |
| A | ASP15 |
| A | TRP16 |
| A | PRO17 |
| A | SER43 |
| A | LEU44 |
| A | PRO45 |
| A | HOH670 |
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 | 4 |
| 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 | 2 |
| 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 | 2 |
| Details | Site: {"description":"Involved in determining product regiospecificity","evidences":[{"source":"PubMed","id":"22203090","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
