Crystal structure of a mycobacterium aldo-keto reductase in its apo and liganded form

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 18% strand (DSSP).

Ligands and binding sites

• NA7 · [(2R,3R,4R,5R)-5-(6-amino-9H-purin-9-yl)-3-hydroxy-4-(phosphonooxy)tetrahydrofuran-2-yl]methyl [(2R,3S,4S)-3,4-dihydroxytetrahydrofuran-2-yl]methyl dihydrogen diphosphate · ligand · 2 copies · chains A, B

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

Pockets

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

Interfaces

1 interface between chains.

• A–B · 141 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

• 2WZM · Crystal structure of a mycobacterium aldo-keto reductase in its apo and liganded form · the same entry in another collection · chain A against A, TM-score 1.00
• A0QV09 · AlphaFold monomer V2.0 prediction for uncharacterized oxidoreductase… · 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 A0QV09
• Elsewhere: RCSB PDB 2WZM · PDBe 2WZM · UniProt A0QV09