The aminoacrylate form of the wild-type salmonella typhimurium tryptophan synthase in complex with inhibitor N-(4'- trifluoromethoxybenzenesulfonyl)-2-amino-1-ethylphosphate (F9F) at the enzyme alpha-site, sodium ion at the metal coordination site and benzimidazole (bzi) at the enzyme beta-site at 1.30 ångström 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

Structure

x-ray diffraction · 2 distinct chains · 48% helix, 19% strand (DSSP).

Ligands and binding sites

• BZI · Benzimidazole · ligand · 2 copies · chains B
• F9F · 2-({[4-(trifluoromethoxy)phenyl]sulfonyl}amino)ethyl dihydrogen phosphate · ligand · chains A, B
• 0JO · 2-{[(E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}prop-2-enoic acid · ligand · chains B
• NA · Sodium ion · metal · chains B
• CL · Chloride ion · ion · chains A
• EDO · 1,2-ethanediol · additive · 5 copies · chains A, B
• PEG · Di(hydroxyethyl)ether · additive · chains B
• PGE · Triethylene glycol · additive · chains B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Interfaces

1 interface between chains.

• A–B · 1412 Ų buried · 28 hydrogen bonds · protein-protein

Compared structures

• 7KXC · The aminoacrylate form of the wild-type Salmonella typhimurium Tryptophan Synthase in… · the same entry in another collection · chain A against A, TM-score 1.00
• P0A2K1 · AlphaFold monomer V2.0 prediction for tryptophan synthase beta chain (P0A2K1) · a predicted model of the same protein · chain B against A, TM-score 1.00

Analyse

• Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
• Every structure of UniProt A0A0D6FWC1
• Every structure of UniProt P0A2K1
• Elsewhere: RCSB PDB 7KXC · PDBe 7KXC · UniProt A0A0D6FWC1 · UniProt P0A2K1