Structural studies reveal the inactivation of E. COLI L-aspartate aminotransferase by (S)-4,5-amino-dihydro-2-thiophenecarboxylic acid (sadta) via two mechanisms (at pH 8.0)

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 14% strand (DSSP).

Ligands and binding sites

• PSZ · 4-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]thiophene-2-carboxylic acid · ligand · chains A
• PMP · 4'-deoxy-4'-aminopyridoxal-5'-phosphate · ligand · chains A
• SO4 · Sulfate ion · ion · 3 copies · chains A
• GOL · Glycerol · additive · 8 copies · chains A

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

Pockets

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

Modifications

Observed in the structure: 1 covalent, 1 modified (covalent ligand, nonstandard).

Compared structures

• 2QBT · Structural Studies Reveal The Inactivation of E. coli L-aspartate aminotransferase by… · the same entry in another collection · chain A against A, TM-score 1.00
• P00509 · AlphaFold monomer V2.0 prediction for aspartate aminotransferase (P00509) · 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 P00509
• Elsewhere: RCSB PDB 2QBT · PDBe 2QBT · UniProt P00509