Tryptophan synthase in complex with gp, alpha-D,L-glycerol- phosphate, cs, PH6.5 - alpha aminoacrylate form - (GP)E(A- a)

Structure

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

Ligands and binding sites

• G3P · Sn-glycerol-3-phosphate · ligand · chains A
• P1T · 2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]acrylic acid · ligand · chains B
• CS · Cesium ion · metal · 3 copies · chains B
• DMS · Dimethyl sulfoxide · additive · 3 copies · chains B, A

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

Pockets

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

Interfaces

1 interface between chains.

• A–B · 1410 Ų buried · 29 hydrogen bonds · protein-protein

Compared structures

• 2J9X · Tryptophan Synthase in complex with GP, alpha-D,L-glycerol-phosphate, Cs, pH6.5 - alpha… · 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
• P00929 · AlphaFold monomer V2.0 prediction for tryptophan synthase alpha chain (P00929) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P00929
• Every structure of UniProt P0A2K1
• Elsewhere: RCSB PDB 2J9X · PDBe 2J9X · UniProt P00929 · UniProt P0A2K1