X-ray crystal structure at 1.65A resolution of human mitochondrial branched chain aminotransferase (bcatm) complexed with a thiazole compound and pmp cofactor.

Structure

x-ray diffraction · 2 distinct chains · 25% helix, 31% strand (DSSP).

Ligands and binding sites

• PMP · 4'-deoxy-4'-aminopyridoxal-5'-phosphate · ligand · 2 copies · chains A, B
• 68C · 5-methyl-4-oxo-N-(1,3,4-thiadiazol-2-yl)-3,4-dihydrothieno[2,3-d]pyrimidine-6-carboxamide · ligand · 2 copies · chains A, B
• CL · Chloride ion · ion · 6 copies · chains A, B
• EDO · 1,2-ethanediol · additive · 11 copies · chains A, B
• GOL · Glycerol · additive · 5 copies · chains A, B

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

Pockets

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

Interfaces

1 interface between chains.

• A–B · 2364 Ų buried · 33 hydrogen bonds · protein-protein

Compared structures

• 5I5X · X-ray crystal structure at 1.65A resolution of human mitochondrial branched chain… · the same entry in another collection · chain A against A, TM-score 1.00
• O15382 · AlphaFold monomer V2.0 prediction for branched-chain-amino-acid aminotransferase… · a predicted model of the same protein · chain A 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 O15382
• Elsewhere: RCSB PDB 5I5X · PDBe 5I5X · UniProt O15382