2VZM
Crystal structure of the narbomycin-bound PikC D50N mutant
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 | 0033068 | biological_process | macrolide biosynthetic process |
| 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 | 0033068 | biological_process | macrolide biosynthetic process |
| 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 1407 |
| Chain | Residue |
| A | MET92 |
| A | THR248 |
| A | LEU251 |
| A | PRO289 |
| A | ALA293 |
| A | THR294 |
| A | ARG296 |
| A | ALA346 |
| A | PHE347 |
| A | GLY348 |
| A | ILE351 |
| A | LEU93 |
| A | HIS352 |
| A | CYS354 |
| A | ILE355 |
| A | GLY356 |
| A | ALA360 |
| A | HOH2323 |
| A | HIS100 |
| A | ARG104 |
| A | PHE111 |
| A | ILE157 |
| A | ALA243 |
| A | GLY244 |
| A | THR247 |
| site_id | AC2 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE HEM B 1407 |
| Chain | Residue |
| B | LYS72 |
| B | MET92 |
| B | LEU93 |
| B | HIS100 |
| B | ARG104 |
| B | LEU240 |
| B | ALA243 |
| B | GLY244 |
| B | THR247 |
| B | THR248 |
| B | LEU251 |
| B | PRO289 |
| B | ALA293 |
| B | THR294 |
| B | ARG296 |
| B | ALA346 |
| B | PHE347 |
| B | GLY348 |
| B | ILE351 |
| B | HIS352 |
| B | CYS354 |
| B | ILE355 |
| B | GLY356 |
| B | ALA360 |
| B | HOH2316 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE NRB A 1408 |
| Chain | Residue |
| A | GLU85 |
| A | GLU94 |
| A | PHE178 |
| A | MET191 |
| A | HIS238 |
| A | ILE239 |
| A | ALA243 |
| A | GLU246 |
| A | THR294 |
| A | TYR295 |
| A | MET394 |
| A | ILE395 |
| A | HOH2233 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE NRB B 1408 |
| Chain | Residue |
| B | GLU85 |
| B | GLU94 |
| B | PHE178 |
| B | MET191 |
| B | HIS238 |
| B | ILE239 |
| B | ALA243 |
| B | THR294 |
| B | ASN392 |
| B | MET394 |
| B | ILE395 |
| B | HOH2318 |
Functional Information from PROSITE/UniProt
| site_id | PS00086 |
| Number of Residues | 10 |
| Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGhGIHFCIG |
| Chain | Residue | Details |
| A | PHE347-GLY356 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 26 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16825192","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19124459","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"16825192","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19124459","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19833867","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24627965","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2C6H","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"2C7X","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"2CA0","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"2CD8","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"2VZ7","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"2VZM","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"2WHW","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"2WI9","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"3ZK5","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"4B7D","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"4B7S","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"4BF4","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1akd |
| Chain | Residue | Details |
| A | GLU246 | |
| A | THR247 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1akd |
| Chain | Residue | Details |
| B | GLU246 | |
| B | THR247 |
