2JJO
Structure of cytochrome P450 EryK in complex with its natural substrate erD
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 | 0016709 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen |
| A | 0017000 | biological_process | antibiotic biosynthetic process |
| A | 0020037 | molecular_function | heme binding |
| A | 0033068 | biological_process | macrolide biosynthetic process |
| A | 0036199 | molecular_function | cholest-4-en-3-one 26-monooxygenase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050661 | molecular_function | NADP binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE HEM A 412 |
| Chain | Residue |
| A | ILE87 |
| A | THR246 |
| A | LEU249 |
| A | MET291 |
| A | ARG293 |
| A | SER345 |
| A | PHE346 |
| A | GLY347 |
| A | HIS351 |
| A | CYS353 |
| A | GLY355 |
| A | HIS88 |
| A | ALA359 |
| A | EY5413 |
| A | HOH2080 |
| A | HOH2331 |
| A | HOH2332 |
| A | HOH2333 |
| A | HIS95 |
| A | ARG99 |
| A | PHE106 |
| A | LEU238 |
| A | ALA241 |
| A | GLY242 |
| A | THR245 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE EY5 A 413 |
| Chain | Residue |
| A | HIS88 |
| A | GLU89 |
| A | LEU169 |
| A | ILE172 |
| A | MET174 |
| A | PRO177 |
| A | ILE186 |
| A | LEU240 |
| A | ALA241 |
| A | THR245 |
| A | PHE288 |
| A | GLN292 |
| A | HEM412 |
| A | HOH2217 |
| A | HOH2238 |
| A | HOH2332 |
| A | HOH2334 |
| A | HOH2335 |
Functional Information from PROSITE/UniProt
| site_id | PS00086 |
| Number of Residues | 10 |
| Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGhGVHFCLG |
| Chain | Residue | Details |
| A | PHE346-GLY355 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | HIS95 | |
| A | ARG99 | |
| A | GLN292 | |
| A | ARG293 | |
| A | HIS351 | |
| A | HIS88 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | BINDING: axial binding residue |
| Chain | Residue | Details |
| A | CYS353 |
