2NZ5
Structure and Function Studies of Cytochrome P450 158A1 from Streptomyces coelicolor A3(2)
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 | 20 |
| Details | BINDING SITE FOR RESIDUE HEM A 430 |
| Chain | Residue |
| A | ARG74 |
| A | ALA348 |
| A | TYR349 |
| A | GLY350 |
| A | HIS354 |
| A | CYS356 |
| A | THR357 |
| A | 226431 |
| A | HOH495 |
| A | HOH520 |
| A | HOH564 |
| A | LEU96 |
| A | HOH574 |
| A | ALA97 |
| A | HIS104 |
| A | PHE115 |
| A | GLY245 |
| A | ALA248 |
| A | LEU296 |
| A | TYR321 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE 226 A 431 |
| Chain | Residue |
| A | HIS290 |
| A | ARG291 |
| A | LEU296 |
| A | HEM430 |
| A | HOH457 |
| A | HOH497 |
| A | HOH556 |
| A | HOH564 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE 226 A 432 |
| Chain | Residue |
| A | HIS88 |
| A | PHE89 |
| A | LYS90 |
| A | ARG92 |
| A | LYS195 |
| A | TYR199 |
| A | HOH563 |
| site_id | AC4 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE HEM B 430 |
| Chain | Residue |
| B | ARG74 |
| B | LEU96 |
| B | ALA97 |
| B | HIS104 |
| B | PHE115 |
| B | LEU242 |
| B | GLY245 |
| B | ALA248 |
| B | LEU296 |
| B | ALA348 |
| B | TYR349 |
| B | GLY350 |
| B | HIS354 |
| B | CYS356 |
| B | THR357 |
| B | ALA362 |
| B | 226431 |
| B | HOH437 |
| B | HOH447 |
| B | HOH463 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE 226 B 431 |
| Chain | Residue |
| B | ARG291 |
| B | LEU296 |
| B | HEM430 |
| B | HOH442 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE 226 B 432 |
| Chain | Residue |
| B | LYS90 |
| B | ARG92 |
| B | LYS195 |
| B | TYR199 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17614370","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2NZ5","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":"17614370","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2DKK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2NZ5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2NZA","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 |
