2Y5N
Structure of the mixed-function P450 MycG in complex with mycinamicin V 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 | 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE HEM A 450 |
| Chain | Residue |
| A | LEU83 |
| A | GLN242 |
| A | PHE286 |
| A | ARG288 |
| A | GLY338 |
| A | PHE339 |
| A | GLY340 |
| A | HIS344 |
| A | CYS346 |
| A | LEU347 |
| A | GLY348 |
| A | LEU84 |
| A | ALA352 |
| A | MYV460 |
| A | HOH2397 |
| A | HOH2566 |
| A | HOH2567 |
| A | HIS91 |
| A | ARG95 |
| A | PHE102 |
| A | ALA234 |
| A | GLY235 |
| A | SER238 |
| A | THR239 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE MYV A 460 |
| Chain | Residue |
| A | ARG75 |
| A | VAL79 |
| A | GLY81 |
| A | GLY82 |
| A | LEU84 |
| A | PHE168 |
| A | VAL174 |
| A | MET179 |
| A | VAL233 |
| A | ALA234 |
| A | LEU386 |
| A | HEM450 |
| A | HOH2313 |
| A | HOH2399 |
| A | HOH2569 |
| A | HOH2570 |
| A | HOH2571 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 1398 |
| Chain | Residue |
| A | ARG113 |
| A | GLU120 |
| A | ARG145 |
| A | SER155 |
| A | HIS158 |
| A | HOH2572 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 1399 |
| Chain | Residue |
| A | THR18 |
| A | LEU19 |
| A | ALA20 |
| A | GLY21 |
| A | HOH2573 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 1400 |
| Chain | Residue |
| A | GLU292 |
| A | HOH2575 |
| A | HOH2576 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 1401 |
| Chain | Residue |
| A | GLY191 |
| A | ASP195 |
| A | HOH2346 |
| A | HOH2578 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 1402 |
| Chain | Residue |
| A | ARG140 |
| A | THR240 |
| A | THR241 |
| A | ALA244 |
| A | GLY389 |
| A | PRO390 |
| A | LEU391 |
| A | HOH2579 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 1403 |
| Chain | Residue |
| A | ARG140 |
| A | THR171 |
| A | LEU391 |
| A | HOH2311 |
| A | HOH2561 |
| A | HOH2581 |
| A | HOH2582 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 1404 |
| Chain | Residue |
| A | ASP325 |
| A | HOH2483 |
| A | HOH2485 |
| site_id | BC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL A 1405 |
| Chain | Residue |
| A | ARG73 |
| A | THR74 |
| A | VAL282 |
| A | GLY283 |
| A | ALA285 |
| A | MET385 |
| A | LEU386 |
| A | HOH2439 |
| A | HOH2583 |
| A | HOH2584 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 1406 |
| Chain | Residue |
| A | HOH2103 |
| A | HOH2251 |
| A | HOH2260 |
| A | HOH2263 |
| site_id | BC3 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEM B 450 |
| Chain | Residue |
| B | THR239 |
| B | ALA285 |
| B | PHE286 |
| B | ARG288 |
| B | GLY338 |
| B | PHE339 |
| B | GLY340 |
| B | HIS344 |
| B | CYS346 |
| B | GLY348 |
| B | MYV460 |
| B | HOH2381 |
| B | HOH2543 |
| B | LEU83 |
| B | LEU84 |
| B | HIS91 |
| B | ARG95 |
| B | PHE102 |
| B | ALA234 |
| B | GLY235 |
| B | SER238 |
| site_id | BC4 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE MYV B 460 |
| 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 | LEU386 |
| B | HEM450 |
| B | HOH2545 |
| B | HOH2546 |
| B | HOH2547 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 1398 |
| Chain | Residue |
| B | ARG253 |
| B | GLU255 |
| B | ILE327 |
| B | HOH2464 |
| B | HOH2469 |
| site_id | BC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 1399 |
| Chain | Residue |
| B | ARG140 |
| B | THR240 |
| B | THR241 |
| B | ALA244 |
| B | GLY389 |
| B | PRO390 |
| B | LEU391 |
| B | HOH2548 |
| site_id | BC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL B 1400 |
| Chain | Residue |
| B | LEU56 |
| B | GLY57 |
| B | GLY59 |
| B | PHE61 |
| B | PRO88 |
| B | GLY342 |
| B | VAL343 |
| B | HOH2201 |
| B | HOH2549 |
| site_id | BC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL B 1401 |
| Chain | Residue |
| B | THR2 |
| B | ARG34 |
| B | GLU41 |
| B | GLU42 |
| B | ALA43 |
| B | TRP44 |
| B | GLU305 |
| B | PRO306 |
| B | HOH2551 |
| site_id | BC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 1402 |
| Chain | Residue |
| B | TYR248 |
| B | THR252 |
| B | ARG253 |
| B | GLU376 |
| B | HOH2552 |
| B | HOH2553 |
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 | 46 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| 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 | 2 |
| 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 | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22952225","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| 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 |
