5BJW
X-ray structure of the PglF 4,6-dehydratase from campylobacter jejuni, T595S variant, in complex with UDP
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | binding site for residue UDP A 701 |
| Chain | Residue |
| A | LYS397 |
| A | GLU526 |
| A | HOH817 |
| A | HOH821 |
| A | HOH849 |
| A | HOH878 |
| A | HOH944 |
| A | HOH950 |
| A | ASN433 |
| A | SER440 |
| A | VAL441 |
| A | THR456 |
| A | LEU457 |
| A | THR458 |
| A | ILE462 |
| A | ARG464 |
| site_id | AC2 |
| Number of Residues | 35 |
| Details | binding site for residue NAD A 702 |
| Chain | Residue |
| A | GLY278 |
| A | GLY280 |
| A | GLY281 |
| A | THR282 |
| A | ILE283 |
| A | ASP303 |
| A | HIS304 |
| A | SER305 |
| A | ASN308 |
| A | LEU328 |
| A | SER329 |
| A | ILE330 |
| A | ALA351 |
| A | ALA352 |
| A | ALA353 |
| A | LYS355 |
| A | ASN370 |
| A | ILE393 |
| A | SER394 |
| A | LYS409 |
| A | PHE431 |
| A | GLY432 |
| A | ASN433 |
| A | VAL434 |
| A | SER437 |
| A | SER438 |
| A | HOH851 |
| A | HOH863 |
| A | HOH864 |
| A | HOH883 |
| A | HOH889 |
| A | HOH900 |
| A | HOH1024 |
| A | HOH1031 |
| B | HOH855 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 703 |
| Chain | Residue |
| A | GLY280 |
| A | GLY281 |
| A | THR282 |
| A | HOH822 |
| A | HOH835 |
| A | HOH1023 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue NA A 704 |
| Chain | Residue |
| A | LYS320 |
| A | ILE323 |
| A | HOH860 |
| A | HOH1045 |
| A | HOH1048 |
| B | HOH1033 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue NA A 705 |
| Chain | Residue |
| A | HOH896 |
| A | HOH937 |
| A | HOH1013 |
| A | HOH1023 |
| A | HOH1047 |
| A | HOH1083 |
| site_id | AC6 |
| Number of Residues | 36 |
| Details | binding site for residue NAD B 701 |
| Chain | Residue |
| B | HOH901 |
| B | HOH915 |
| B | HOH938 |
| B | HOH986 |
| B | HOH1046 |
| B | HOH1048 |
| A | HOH856 |
| B | GLY278 |
| B | GLY280 |
| B | GLY281 |
| B | THR282 |
| B | ILE283 |
| B | ASP303 |
| B | HIS304 |
| B | SER305 |
| B | ASN308 |
| B | LEU328 |
| B | SER329 |
| B | ILE330 |
| B | ALA351 |
| B | ALA352 |
| B | ALA353 |
| B | LYS355 |
| B | ASN370 |
| B | ILE393 |
| B | SER394 |
| B | LYS409 |
| B | PHE431 |
| B | GLY432 |
| B | ASN433 |
| B | VAL434 |
| B | SER437 |
| B | SER438 |
| B | HOH869 |
| B | HOH884 |
| B | HOH891 |
| site_id | AC7 |
| Number of Residues | 19 |
| Details | binding site for residue UDP B 702 |
| Chain | Residue |
| B | LYS397 |
| B | ASN433 |
| B | SER440 |
| B | VAL441 |
| B | THR456 |
| B | LEU457 |
| B | THR458 |
| B | ILE462 |
| B | ARG464 |
| B | GLU526 |
| B | EDO705 |
| B | HOH836 |
| B | HOH851 |
| B | HOH883 |
| B | HOH884 |
| B | HOH892 |
| B | HOH899 |
| B | HOH900 |
| B | HOH982 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 703 |
| Chain | Residue |
| B | GLY280 |
| B | GLY281 |
| B | HOH822 |
| B | HOH823 |
| B | HOH1068 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 704 |
| Chain | Residue |
| A | HOH957 |
| B | TYR307 |
| B | LYS311 |
| B | HOH829 |
| B | HOH1020 |
| site_id | AD1 |
| Number of Residues | 8 |
| Details | binding site for residue EDO B 705 |
| Chain | Residue |
| B | LYS355 |
| B | HIS356 |
| B | SER437 |
| B | SER438 |
| B | SER440 |
| B | UDP702 |
| B | HOH884 |
| B | HOH982 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue NA B 706 |
| Chain | Residue |
| B | ASP261 |
| B | SER263 |
| B | HOH954 |
| B | HOH1019 |
| B | HOH1054 |
| B | HOH1110 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue NA B 707 |
| Chain | Residue |
| B | HOH878 |
| B | HOH953 |
| B | HOH1035 |
| B | HOH1068 |
| B | HOH1078 |
