3ZPI
PikC D50N mutant 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 | 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 | 3 |
| Details | BINDING SITE FOR RESIDUE FMT B 1408 |
| Chain | Residue |
| B | ASP222 |
| B | HOH2294 |
| B | HOH2296 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE TLA A 1419 |
| Chain | Residue |
| A | HOH2468 |
| B | ARG60 |
| B | ARG69 |
| B | ASP303 |
| B | HOH2083 |
| A | PRO30 |
| A | ARG34 |
| A | EDO1415 |
| A | HOH2464 |
| A | HOH2465 |
| A | HOH2466 |
| site_id | AC3 |
| 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 | PHE111 |
| 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 | HIS352 |
| B | CYS354 |
| B | ILE355 |
| B | GLY356 |
| B | ALA360 |
| B | HOH2312 |
| B | HOH2385 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 1409 |
| Chain | Residue |
| B | GLY343 |
| B | HIS344 |
| B | ARG361 |
| B | EDO1410 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 1410 |
| Chain | Residue |
| B | ARG62 |
| B | GLY343 |
| B | HIS344 |
| B | EDO1409 |
| site_id | AC6 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE HEM A 1407 |
| Chain | Residue |
| A | LYS72 |
| A | MET92 |
| A | LEU93 |
| A | HIS100 |
| A | ARG104 |
| A | PHE111 |
| A | ALA243 |
| A | GLY244 |
| A | THR247 |
| A | THR248 |
| A | LEU251 |
| A | PRO289 |
| A | ALA293 |
| A | THR294 |
| A | ARG296 |
| A | ALA346 |
| A | PHE347 |
| A | GLY348 |
| A | HIS352 |
| A | CYS354 |
| A | ILE355 |
| A | GLY356 |
| A | ALA360 |
| A | HOH2365 |
| A | HOH2434 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FMT A 1408 |
| Chain | Residue |
| A | ARG104 |
| A | ILE351 |
| A | HOH2469 |
| A | HOH2470 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE FMT A 1409 |
| Chain | Residue |
| A | ASP167 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 1410 |
| Chain | Residue |
| A | GLU223 |
| A | EDO1411 |
| A | HOH2343 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 1411 |
| Chain | Residue |
| A | GLU223 |
| A | ASP224 |
| A | EDO1410 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE FMT A 1412 |
| Chain | Residue |
| A | ARG270 |
| A | MET273 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FMT A 1413 |
| Chain | Residue |
| A | PRO330 |
| A | ASP336 |
| A | ARG339 |
| A | HOH2420 |
| site_id | BC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE FMT B 1411 |
| Chain | Residue |
| B | GLY350 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FMT B 1412 |
| Chain | Residue |
| B | ASP209 |
| B | HOH2280 |
| B | HOH2282 |
| B | HOH2405 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 1414 |
| Chain | Residue |
| A | ARG122 |
| A | VAL156 |
| A | GLU159 |
| A | HOH2472 |
| site_id | BC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 1415 |
| Chain | Residue |
| A | PHE24 |
| A | ASP27 |
| A | PRO30 |
| A | TLA1419 |
| A | HOH2040 |
| A | HOH2473 |
| A | ASP23 |
| site_id | BC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE FMT A 1416 |
| Chain | Residue |
| A | MET145 |
| A | ARG172 |
| A | ASP176 |
| site_id | BC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO A 1417 |
| Chain | Residue |
| A | TYR29 |
| A | ARG324 |
| A | HIS333 |
| A | HOH2046 |
| A | HOH2395 |
| A | HOH2474 |
| B | ASP303 |
| B | GLY306 |
| B | VAL308 |
| site_id | CC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE NA A 1418 |
| Chain | Residue |
| A | GLU291 |
| A | TYR390 |
| A | PRO391 |
| A | ASN392 |
| A | ILE395 |
| A | HOH2033 |
| A | HOH2401 |
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 |






