Apo form of the E124S mutant of betaine aldehyde dehydrogenase from pseudomonas aeruginosa

Structure

x-ray diffraction · 4 distinct chains · 42% helix, 21% strand (DSSP).

Ligands and binding sites

• K · Potassium ion · metal · 4 copies · chains A, B, C, D
• EDO · 1,2-ethanediol · additive · 8 copies · chains A, D, B
• GOL · Glycerol · additive · 3 copies · chains A

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

Pockets

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

Interfaces

5 interfaces between chains.

• B–C · 2658 Ų buried · 45 hydrogen bonds · protein-protein
• A–D · 2617 Ų buried · 50 hydrogen bonds · protein-protein
• A–C · 275 Ų buried · 7 hydrogen bonds · protein-protein
• B–D · 231 Ų buried · 1 hydrogen bond · protein-protein
• A–B · 169 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (oxidation).

Compared structures

• 6BJP · Apo form of the E124S mutant of betaine aldehyde dehydrogenase from Pseudomonas aeruginosa · the same entry in another collection · chain A against A, TM-score 1.00
• Q9HTJ1 · AlphaFold monomer V2.0 prediction for NAD/NADP-dependent betaine aldehyde dehydrogenase… · a predicted model of the same protein · chain D against A, TM-score 0.96

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 Q9HTJ1
• Elsewhere: RCSB PDB 6BJP · PDBe 6BJP · UniProt Q9HTJ1