2YGX
Structure of the mixed-function P450 MycG in P21 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 |
| C | 0004497 | molecular_function | monooxygenase activity |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0006707 | biological_process | cholesterol catabolic process |
| C | 0008395 | molecular_function | steroid hydroxylase activity |
| C | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| C | 0017000 | biological_process | antibiotic biosynthetic process |
| C | 0020037 | molecular_function | heme binding |
| C | 0036199 | molecular_function | cholest-4-en-3-one 26-monooxygenase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0055114 | biological_process | obsolete oxidation-reduction process |
| D | 0004497 | molecular_function | monooxygenase activity |
| D | 0005506 | molecular_function | iron ion binding |
| D | 0006707 | biological_process | cholesterol catabolic process |
| D | 0008395 | molecular_function | steroid hydroxylase activity |
| D | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| D | 0017000 | biological_process | antibiotic biosynthetic process |
| D | 0020037 | molecular_function | heme binding |
| D | 0036199 | molecular_function | cholest-4-en-3-one 26-monooxygenase activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0055114 | biological_process | obsolete oxidation-reduction process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL D 1398 |
| Chain | Residue |
| D | VAL135 |
| D | ARG140 |
| D | THR240 |
| D | THR241 |
| D | ALA244 |
| D | GLY389 |
| D | PRO390 |
| D | HOH2061 |
| site_id | AC2 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE HEM A 450 |
| Chain | Residue |
| A | LEU84 |
| A | HIS91 |
| A | ARG95 |
| A | PHE102 |
| A | LEU231 |
| A | ALA234 |
| A | GLY235 |
| A | SER238 |
| A | THR239 |
| A | PHE286 |
| A | ARG288 |
| A | GLY338 |
| A | PHE339 |
| A | GLY340 |
| A | HIS344 |
| A | CYS346 |
| A | GLY348 |
| A | HOH2074 |
| A | HOH2104 |
| A | LEU83 |
| 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 | LEU231 |
| B | ALA234 |
| B | GLY235 |
| B | SER238 |
| B | THR239 |
| B | GLN242 |
| B | ALA285 |
| B | PHE286 |
| B | ARG288 |
| B | GLY338 |
| B | PHE339 |
| B | GLY340 |
| B | HIS344 |
| B | CYS346 |
| B | GLY348 |
| B | ALA352 |
| B | HOH2066 |
| B | HOH2093 |
| site_id | AC4 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEM C 450 |
| Chain | Residue |
| C | LEU83 |
| C | LEU84 |
| C | HIS91 |
| C | ARG95 |
| C | PHE102 |
| C | ALA234 |
| C | GLY235 |
| C | SER238 |
| C | THR239 |
| C | PHE286 |
| C | ARG288 |
| C | GLY338 |
| C | PHE339 |
| C | GLY340 |
| C | HIS344 |
| C | CYS346 |
| C | GLY348 |
| C | ALA352 |
| C | LEU356 |
| C | HOH2073 |
| C | HOH2099 |
| site_id | AC5 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEM D 450 |
| Chain | Residue |
| D | LEU83 |
| D | LEU84 |
| D | HIS91 |
| D | ARG95 |
| D | ALA234 |
| D | GLY235 |
| D | SER238 |
| D | THR239 |
| D | GLN242 |
| D | ALA285 |
| D | PHE286 |
| D | ARG288 |
| D | GLY338 |
| D | PHE339 |
| D | GLY340 |
| D | HIS344 |
| D | CYS346 |
| D | GLY348 |
| D | ALA352 |
| D | HOH2069 |
| D | HOH2098 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 1398 |
| Chain | Residue |
| A | LEU56 |
| A | GLY59 |
| A | PRO88 |
| A | VAL343 |
| A | HOH2027 |
| A | HOH2113 |
| B | ASP325 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 1399 |
| Chain | Residue |
| A | GLY81 |
| A | GLY82 |
| A | LEU83 |
| A | LEU84 |
| A | GLY230 |
| A | VAL233 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 1400 |
| Chain | Residue |
| A | ARG140 |
| A | THR240 |
| A | THR241 |
| A | GLY389 |
| A | PRO390 |
| A | LEU391 |
| A | HOH2065 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 1401 |
| Chain | Residue |
| A | ARG253 |
| A | GLU255 |
| A | GLN259 |
| A | ILE327 |
| A | HOH2080 |
| A | HOH2100 |
| B | GLU292 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 1398 |
| Chain | Residue |
| A | GLY342 |
| B | GLY21 |
| B | GLY24 |
| B | GLU25 |
| B | ASP325 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SIN B 1399 |
| Chain | Residue |
| B | GLU5 |
| B | ARG34 |
| B | GLU305 |
| site_id | BC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 1400 |
| Chain | Residue |
| A | ASP325 |
| B | LEU56 |
| B | GLY57 |
| B | ASP58 |
| B | PRO88 |
| B | VAL343 |
| B | HOH2026 |
| B | HOH2102 |
| site_id | BC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL B 1401 |
| Chain | Residue |
| B | VAL135 |
| B | ARG140 |
| B | THR240 |
| B | THR241 |
| B | ALA244 |
| B | GLY389 |
| B | PRO390 |
| B | LEU391 |
| B | HOH2055 |
| site_id | BC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL C 1398 |
| Chain | Residue |
| C | LEU56 |
| C | GLY57 |
| C | GLY59 |
| C | PRO88 |
| C | VAL343 |
| C | HOH2022 |
| C | HOH2108 |
| D | ASP325 |
| site_id | BC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL C 1399 |
| Chain | Residue |
| C | ARG140 |
| C | THR240 |
| C | THR241 |
| C | ALA244 |
| C | GLY389 |
| C | PRO390 |
| C | LEU391 |
| C | HOH2062 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL C 1400 |
| Chain | Residue |
| C | ARG253 |
| C | GLU255 |
| C | ILE327 |
| C | HOH2076 |
| C | HOH2095 |
| D | GLU292 |
| site_id | BC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL D 1399 |
| Chain | Residue |
| C | ASP325 |
| C | HOH2089 |
| C | HOH2092 |
| D | LEU56 |
| D | GLY59 |
| D | PHE61 |
| D | PRO88 |
| D | VAL343 |
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 | 4 |
| 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 | |
| C | GLY81 | |
| D | GLY81 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22952225 |
| Chain | Residue | Details |
| B | HIS91 | |
| B | ARG95 | |
| B | ARG288 | |
| B | HIS344 | |
| C | HIS91 | |
| C | ARG95 | |
| C | ARG288 | |
| C | HIS344 | |
| D | HIS91 | |
| D | ARG95 | |
| D | ARG288 | |
| D | HIS344 | |
| A | HIS91 | |
| A | ARG95 | |
| A | ARG288 | |
| A | HIS344 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| 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 | |
| C | CYS346 | |
| D | CYS346 |
