4AW3
Structure of the mixed-function P450 MycG F286V mutant in complex with mycinamicin V in P1 space group
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 | 25 |
| Details | BINDING SITE FOR RESIDUE HEM A 450 |
| Chain | Residue |
| A | LEU83 |
| A | THR239 |
| A | GLN242 |
| A | ALA285 |
| A | VAL286 |
| A | ARG288 |
| A | GLY338 |
| A | PHE339 |
| A | GLY340 |
| A | HIS344 |
| A | CYS346 |
| A | LEU84 |
| A | GLY348 |
| A | ALA352 |
| A | MYV500 |
| A | HOH2178 |
| A | HOH2207 |
| A | HOH2235 |
| A | HIS91 |
| A | ARG95 |
| A | PHE102 |
| A | LEU231 |
| A | ALA234 |
| A | GLY235 |
| A | SER238 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE MYV A 500 |
| Chain | Residue |
| A | ARG75 |
| A | GLU77 |
| A | VAL79 |
| A | GLY81 |
| A | GLY82 |
| A | LEU83 |
| A | LEU84 |
| A | PHE168 |
| A | VAL174 |
| A | ALA176 |
| A | MET179 |
| A | VAL233 |
| A | ALA234 |
| A | GLU237 |
| A | LEU386 |
| A | HEM450 |
| A | HOH2080 |
| A | HOH2147 |
| A | HOH2148 |
| A | HOH2153 |
| A | HOH2176 |
| A | HOH2207 |
| site_id | AC3 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEM B 450 |
| Chain | Residue |
| B | LEU83 |
| B | LEU84 |
| B | HIS91 |
| B | ARG95 |
| B | PHE102 |
| B | LEU231 |
| B | ALA234 |
| B | GLY235 |
| B | SER238 |
| B | THR239 |
| B | VAL286 |
| B | ARG288 |
| B | GLY338 |
| B | PHE339 |
| B | GLY340 |
| B | HIS344 |
| B | CYS346 |
| B | GLY348 |
| B | MYV500 |
| B | HOH2168 |
| B | HOH2193 |
| B | HOH2215 |
| site_id | AC4 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE MYV B 500 |
| Chain | Residue |
| B | ARG75 |
| B | GLU77 |
| B | VAL79 |
| B | GLY81 |
| B | GLY82 |
| B | LEU83 |
| B | LEU84 |
| B | PHE168 |
| B | SER170 |
| B | VAL174 |
| B | MET179 |
| B | VAL233 |
| B | ALA234 |
| B | GLU237 |
| B | LEU386 |
| B | LEU387 |
| B | HEM450 |
| B | HOH2145 |
| B | HOH2146 |
| B | HOH2193 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1398 |
| Chain | Residue |
| A | THR18 |
| A | ARG253 |
| A | HOH2017 |
| A | HOH2185 |
| B | ALA20 |
| B | GLY21 |
| B | ARG22 |
| B | HOH2010 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1398 |
| Chain | Residue |
| A | PRO350 |
| A | ARG353 |
| A | HOH2240 |
| A | HIS345 |
| A | ALA349 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1399 |
| Chain | Residue |
| A | ARG95 |
| A | HIS345 |
| A | HOH2098 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1400 |
| Chain | Residue |
| A | PRO154 |
| A | ARG196 |
| A | ARG197 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1399 |
| Chain | Residue |
| A | ARG7 |
| B | ARG253 |
| B | PRO254 |
| B | GLU255 |
| B | LEU256 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1400 |
| Chain | Residue |
| B | HIS345 |
| B | PRO350 |
| B | ARG353 |
| B | HOH2219 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1401 |
| Chain | Residue |
| B | ARG95 |
| B | HIS345 |
| B | HOH2088 |
| B | HOH2089 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1401 |
| Chain | Residue |
| A | ALA20 |
| A | GLY21 |
| A | ARG22 |
| A | HOH2021 |
| B | ARG253 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 1402 |
| Chain | Residue |
| B | PRO72 |
| B | ARG73 |
| B | THR74 |
| B | THR284 |
| B | HOH2190 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 1402 |
| Chain | Residue |
| A | PRO72 |
| A | ARG73 |
| A | THR284 |
| site_id | BC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 1403 |
| Chain | Residue |
| B | ARG140 |
| B | THR240 |
| B | THR241 |
| B | ALA244 |
| B | GLY389 |
| B | PRO390 |
| B | LEU391 |
| B | HOH2149 |
| site_id | BC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 1403 |
| Chain | Residue |
| A | ARG140 |
| A | THR240 |
| A | ALA244 |
| A | GLY389 |
| A | PRO390 |
| A | LEU391 |
| A | HOH2152 |
Functional Information from PROSITE/UniProt
| site_id | PS00086 |
| Number of Residues | 10 |
| Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGhGVHHCLG |
| Chain | Residue | Details |
| A | PHE339-GLY348 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22952225, ECO:0007744|PDB:2Y46, ECO:0007744|PDB:2Y98, ECO:0007744|PDB:3ZSN |
| Chain | Residue | Details |
| A | GLY81 | |
| B | GLY81 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22952225 |
| Chain | Residue | Details |
| A | ARG288 | |
| A | HIS344 | |
| B | HIS91 | |
| B | ARG95 | |
| B | ARG288 | |
| B | HIS344 | |
| A | HIS91 | |
| A | ARG95 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: axial binding residue => ECO:0000269|PubMed:22952225, ECO:0007744|PDB:2Y5N, ECO:0007744|PDB:2Y98, ECO:0007744|PDB:2YCA |
| Chain | Residue | Details |
| A | CYS346 | |
| B | CYS346 |
