7LY8
The internal aldimine form of the wild-type Salmonella Typhimurium Tryptophan Synthase in complex with two molecules of N-(4'-trifluoromethoxybenzoyl)-2-amino-1-ethylphosphate (F6F) inhibitor at the enzyme alpha-site, a single F6F molecule at the enzyme beta-site, and sodium ion at the metal coordination site at 1.55 Angstrom resolution. One of the beta-Q114 rotamer conformations allows a hydrogen bond to form with the PLP oxygen at the position 3 in the ring
Summary for 7LY8
Entry DOI | 10.2210/pdb7ly8/pdb |
Related | 4KKX 4WX2 4Y6G 4ZQC 5BW6 7KU9 |
Descriptor | Tryptophan synthase alpha chain, Tryptophan synthase beta chain, 2-{[4-(TRIFLUOROMETHOXY)BENZOYL]AMINO}ETHYL DIHYDROGEN PHOSPHATE, ... (9 entities in total) |
Functional Keywords | inhibitor, internal aldimine, lyase, lyase-lyase inhibitor complex, lyase/lyase inhibitor |
Biological source | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) More |
Total number of polymer chains | 2 |
Total formula weight | 73406.96 |
Authors | Hilario, E.,Dunn, M.F.,Mueller, L.J. (deposition date: 2021-03-06, release date: 2022-03-09, Last modification date: 2023-10-18) |
Primary citation | Hilario, E.,Dunn, M.F.,Mueller, L.J. The internal aldimine form of the wild-type Salmonella Typhimurium Tryptophan Synthase in complex with two molecules of N-(4'-trifluoromethoxybenzoyl)-2-amino-1-ethylphosphate (F6F) inhibitor at the enzyme alpha-site, a single F6F molecule at the enzyme beta-site, and sodium ion at the metal coordination site at 1.55 Angstrom resolution. One of the beta-Q114 rotamer conformations allows a hydrogen bond to form with the PLP oxygen at the position 3 in the ring. To be Published, |
Experimental method | X-RAY DIFFRACTION (1.55 Å) |
Structure validation
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