5FOI
Crystal structure of mycinamicin VIII C21 methyl hydroxylase MycCI from Micromonospora griseorubida bound to mycinamicin VIII
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 | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| A | 0017000 | biological_process | antibiotic biosynthetic process |
| A | 0020037 | molecular_function | heme binding |
| A | 0036199 | molecular_function | cholest-4-en-3-one 26-monooxygenase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0055114 | biological_process | obsolete oxidation-reduction process |
| 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 | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| B | 0017000 | biological_process | antibiotic biosynthetic process |
| B | 0020037 | molecular_function | heme binding |
| B | 0036199 | molecular_function | cholest-4-en-3-one 26-monooxygenase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0055114 | biological_process | obsolete oxidation-reduction process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEM A 413 |
| Chain | Residue |
| A | MET79 |
| A | ALA274 |
| A | LEU277 |
| A | ARG279 |
| A | LEU302 |
| A | ALA329 |
| A | PHE330 |
| A | GLY331 |
| A | HIS335 |
| A | CYS337 |
| A | GLY339 |
| A | LEU80 |
| A | GOL1389 |
| A | HOH2071 |
| A | HIS87 |
| A | ARG91 |
| A | LEU224 |
| A | GLY228 |
| A | THR231 |
| A | SER232 |
| A | LEU268 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE MY8 A 414 |
| Chain | Residue |
| A | ALA69 |
| A | GLY71 |
| A | PHE76 |
| A | LEU80 |
| A | MET81 |
| A | ALA164 |
| A | PRO167 |
| A | SER172 |
| A | MET173 |
| A | LEU223 |
| A | GOL1389 |
| A | HOH2028 |
| A | HOH2076 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE HEM B 413 |
| Chain | Residue |
| B | MET79 |
| B | LEU80 |
| B | HIS87 |
| B | ARG91 |
| B | PHE98 |
| B | ILE143 |
| B | LEU224 |
| B | ALA227 |
| B | THR231 |
| B | LEU277 |
| B | ARG279 |
| B | ALA329 |
| B | PHE330 |
| B | HIS335 |
| B | CYS337 |
| B | MY8414 |
| B | HOH2065 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE MY8 B 414 |
| Chain | Residue |
| B | ALA69 |
| B | GLY71 |
| B | ASP72 |
| B | LEU80 |
| B | ALA164 |
| B | PRO167 |
| B | SER172 |
| B | MET173 |
| B | LEU223 |
| B | HEM413 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 1389 |
| Chain | Residue |
| A | LEU277 |
| A | ARG278 |
| A | PRO377 |
| A | HEM413 |
| A | MY8414 |
| A | HOH2029 |
| A | HOH2062 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 1390 |
| Chain | Residue |
| A | GLN256 |
| A | PRO257 |
| A | GLU258 |
| B | ARG91 |
| B | ILE95 |
| B | HOH2022 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SPD A 1391 |
| Chain | Residue |
| A | ASP153 |
| A | PHE156 |
| A | GLU178 |
| A | GLU181 |
| A | SPD1392 |
| A | SPD1393 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE SPD A 1393 |
| Chain | Residue |
| A | SPD1391 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SPD A 1392 |
| Chain | Residue |
| A | PHE156 |
| A | GLU181 |
| A | SPD1391 |
| B | GLU178 |
Functional Information from PROSITE/UniProt
| site_id | PS00086 |
| Number of Residues | 10 |
| Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGyGPHQCLG |
| Chain | Residue | Details |
| A | PHE330-GLY339 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P18326 |
| Chain | Residue | Details |
| A | ARG279 | |
| A | HIS335 | |
| B | HIS87 | |
| B | ARG91 | |
| B | ARG279 | |
| B | HIS335 | |
| A | HIS87 | |
| A | ARG91 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: axial binding residue => ECO:0000250|UniProtKB:P18326 |
| Chain | Residue | Details |
| A | CYS337 | |
| B | CYS337 |
