2Y98
Structure of the mixed-function P450 MycG in complex with mycinamicin IV in P21212 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 |
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 | SER238 |
| A | THR239 |
| A | GLN242 |
| A | ALA285 |
| A | PHE286 |
| A | ARG288 |
| A | GLY338 |
| A | PHE339 |
| A | GLY340 |
| A | HIS344 |
| A | LEU84 |
| A | CYS346 |
| A | GLY348 |
| A | ALA352 |
| A | MIV460 |
| A | HOH2248 |
| A | HOH2388 |
| A | HIS91 |
| A | ARG95 |
| A | PHE102 |
| A | ILE147 |
| A | LEU231 |
| A | ALA234 |
| A | GLY235 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE MIV A 460 |
| Chain | Residue |
| A | ARG75 |
| A | GLU77 |
| A | VAL79 |
| A | GLY81 |
| A | GLY82 |
| A | LEU84 |
| A | PHE168 |
| A | SER170 |
| A | VAL174 |
| A | VAL233 |
| A | ALA234 |
| A | LEU386 |
| A | HEM450 |
| A | HOH2206 |
| A | HOH2389 |
| A | HOH2390 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 1398 |
| Chain | Residue |
| A | ARG145 |
| A | HIS158 |
| A | HOH2156 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1399 |
| Chain | Residue |
| A | ARG48 |
| A | LYS100 |
| A | ARG297 |
| A | HOH2391 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1400 |
| Chain | Residue |
| A | ALA20 |
| A | GLY21 |
| A | ARG22 |
| A | ARG53 |
| A | GLN335 |
| A | HIS341 |
| A | HOH2065 |
| A | HOH2393 |
| A | HOH2394 |
| A | HOH2395 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL A 1401 |
| Chain | Residue |
| A | LEU56 |
| A | GLY57 |
| A | GLY59 |
| A | PRO88 |
| A | ASP325 |
| A | GLY342 |
| A | VAL343 |
| A | HOH2116 |
| A | HOH2320 |
| A | HOH2396 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 1402 |
| Chain | Residue |
| A | ARG140 |
| A | THR240 |
| A | ALA244 |
| A | GLY389 |
| A | PRO390 |
| A | LEU391 |
| A | HOH2397 |
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 | 23 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| 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 | 1 |
| 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 | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22952225","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| 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 |






