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 | 0006707 | biological_process | cholesterol catabolic process |
A | 0008395 | molecular_function | steroid hydroxylase 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 | 0020037 | molecular_function | heme binding |
A | 0036199 | molecular_function | cholest-4-en-3-one 26-monooxygenase activity |
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 | 0006707 | biological_process | cholesterol catabolic process |
B | 0008395 | molecular_function | steroid hydroxylase activity |
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 | 0036199 | molecular_function | cholest-4-en-3-one 26-monooxygenase activity |
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: BINDING => ECO:0000269|PubMed:15659395, ECO:0000269|PubMed:16239228, ECO:0007744|PDB:1T93, ECO:0007744|PDB:2D09 |
Chain | Residue | Details |
A | ARG288 | |
A | LEU293 | |
B | ARG288 | |
B | LEU293 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: axial binding residue => ECO:0000269|PubMed:15659395, ECO:0000269|PubMed:16239228, ECO:0000269|PubMed:22203090, ECO:0007744|PDB:1S1F, ECO:0007744|PDB:1SE6, ECO:0007744|PDB:1T93, ECO:0007744|PDB:2D09, ECO:0007744|PDB:2D0E, ECO:0007744|PDB:3TZO |
Chain | Residue | Details |
A | CYS353 | |
B | CYS353 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | SITE: Involved in determining product regiospecificity => ECO:0000269|PubMed:22203090 |
Chain | Residue | Details |
A | ILE87 | |
B | ILE87 |