3ZSN
Structure of the mixed-function P450 MycG F286A mutant in complex with mycinamicin IV
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 | 0017000 | biological_process | antibiotic biosynthetic process |
| A | 0020037 | molecular_function | heme binding |
| 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 | 0016491 | molecular_function | oxidoreductase 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 | 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 | 0016491 | molecular_function | oxidoreductase 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 | 0046872 | molecular_function | metal ion binding |
| C | 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 450 |
| Chain | Residue |
| A | LEU83 |
| A | ALA286 |
| A | ARG288 |
| A | GLY338 |
| A | PHE339 |
| A | GLY340 |
| A | HIS344 |
| A | CYS346 |
| A | GLY348 |
| A | MIV460 |
| A | HOH2221 |
| A | LEU84 |
| A | HOH2258 |
| A | HOH2310 |
| A | HIS91 |
| A | ARG95 |
| A | PHE102 |
| A | ALA234 |
| A | GLY235 |
| A | SER238 |
| A | THR239 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE MIV A 460 |
| Chain | Residue |
| A | ARG75 |
| A | VAL79 |
| A | GLY81 |
| A | GLY82 |
| A | LEU84 |
| A | SER170 |
| A | VAL174 |
| A | ALA176 |
| A | MET179 |
| A | VAL233 |
| A | ALA234 |
| A | GLU237 |
| A | LEU386 |
| A | HEM450 |
| A | HOH2110 |
| site_id | AC3 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEM B 450 |
| Chain | Residue |
| B | LEU83 |
| B | LEU84 |
| B | HIS91 |
| B | ARG95 |
| B | PHE102 |
| B | ALA234 |
| B | GLY235 |
| B | SER238 |
| B | THR239 |
| B | ALA285 |
| B | ALA286 |
| B | ARG288 |
| B | GLY338 |
| B | PHE339 |
| B | GLY340 |
| B | HIS344 |
| B | CYS346 |
| B | GLY348 |
| B | HOH2235 |
| B | HOH2269 |
| B | HOH2313 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE MIV B 460 |
| Chain | Residue |
| B | VAL79 |
| B | GLY81 |
| B | GLY82 |
| B | LEU84 |
| B | PHE168 |
| B | SER170 |
| B | VAL174 |
| B | MET179 |
| B | VAL233 |
| B | ALA234 |
| B | GLU237 |
| B | LEU386 |
| B | HOH2125 |
| site_id | AC5 |
| 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 | ALA286 |
| C | ARG288 |
| C | GLY338 |
| C | PHE339 |
| C | GLY340 |
| C | HIS344 |
| C | CYS346 |
| C | GLY348 |
| C | MIV460 |
| C | HOH2235 |
| C | HOH2274 |
| C | HOH2314 |
| site_id | AC6 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE MIV C 460 |
| Chain | Residue |
| C | MET179 |
| C | GLY230 |
| C | VAL233 |
| C | ALA234 |
| C | GLU237 |
| C | LEU386 |
| C | HEM450 |
| C | GLU77 |
| C | VAL79 |
| C | GLY81 |
| C | GLY82 |
| C | LEU84 |
| C | SER170 |
| C | VAL174 |
| C | ALA176 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE BEN A 1398 |
| Chain | Residue |
| A | HIS119 |
| A | ARG366 |
| A | HOH2155 |
| A | HOH2338 |
| B | HIS119 |
| B | ARG366 |
| B | BEN1398 |
| B | HOH2176 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE BEN B 1398 |
| Chain | Residue |
| A | HIS119 |
| A | ARG366 |
| A | BEN1398 |
| A | HOH2155 |
| A | HOH2338 |
| B | HIS119 |
| B | GLN365 |
| B | ARG366 |
| B | HOH2176 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE BEN C 1398 |
| Chain | Residue |
| C | HIS119 |
| C | HIS119 |
| C | ARG366 |
| C | ARG366 |
| C | HOH2174 |
| C | HOH2174 |
| C | HOH2343 |
| C | HOH2343 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 1399 |
| Chain | Residue |
| A | ARG140 |
| A | THR240 |
| A | THR241 |
| A | ALA244 |
| A | GLY389 |
| A | PRO390 |
| A | HOH2191 |
| site_id | BC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GOL C 1399 |
| Chain | Residue |
| A | ASP325 |
| A | HOH2281 |
| A | HOH2292 |
| C | LEU56 |
| C | GLY57 |
| C | GLY59 |
| C | PHE61 |
| C | PRO88 |
| C | GLY342 |
| C | VAL343 |
| C | HOH2127 |
| site_id | BC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE GOL A 1400 |
| Chain | Residue |
| A | LEU56 |
| A | GLY57 |
| A | ASP58 |
| A | GLY59 |
| A | PHE61 |
| A | PRO88 |
| A | GLY342 |
| A | VAL343 |
| A | HOH2114 |
| C | ASP325 |
| C | HOH2288 |
| C | HOH2299 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE BEN B 1399 |
| Chain | Residue |
| A | PRO201 |
| A | THR202 |
| A | ASP203 |
| B | PRO201 |
| B | ASP203 |
| site_id | BC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 1400 |
| Chain | Residue |
| B | ARG140 |
| B | THR240 |
| B | THR241 |
| B | ALA244 |
| B | GLY389 |
| B | PRO390 |
| B | HOH2208 |
| B | HOH2236 |
| site_id | BC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL C 1400 |
| Chain | Residue |
| C | ARG140 |
| C | THR240 |
| C | THR241 |
| C | ALA244 |
| C | GLY389 |
| C | PRO390 |
| C | LEU391 |
| C | HOH2207 |
| site_id | BC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 1401 |
| Chain | Residue |
| A | ARG253 |
| A | GLU255 |
| A | GLN259 |
| A | ILE327 |
| A | HOH2238 |
| A | HOH2239 |
| A | HOH2297 |
| C | GLU292 |
| site_id | BC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 1401 |
| Chain | Residue |
| B | ARG253 |
| B | GLU255 |
| B | GLN259 |
| B | GLU292 |
| B | ILE327 |
| B | HOH2243 |
| B | HOH2249 |
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 | 69 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 30 |
| Details | Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22952225","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2Y46","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2Y98","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ZSN","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22952225","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"22952225","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2Y5N","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2Y98","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2YCA","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
