Apo form of betaine aldehyde dehydrogenase from pseudomonas aeruginosa

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 22% strand (DSSP).

Ligands and binding sites

• K · Potassium ion · metal · 24 copies · chains A, B, C, D, E, F, G, H
• GOL · Glycerol · additive · 22 copies · chains A, C, B, D, F, E, G, H
• EDO · 1,2-ethanediol · additive · 10 copies · chains A, B, C, D, E, F, G
• DTT · 2,3-dihydroxy-1,4-dithiobutane · additive · 8 copies · chains A, B, C, D, E, F, G, H
• PE4 · 2-{2-[2-(2-{2-[2-(2-ethoxy-ethoxy)-ethoxy]-ethoxy}-ethoxy)-ethoxy]-ethoxy}-ethanol · additive · 8 copies · chains A, B, C, D, E, F, G, H

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

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Interfaces

14 interfaces between chains.

• G–H · 3555 Ų buried · 58 hydrogen bonds · protein-protein
• C–D · 3543 Ų buried · 56 hydrogen bonds · protein-protein
• A–B · 3542 Ų buried · 56 hydrogen bonds · protein-protein
• E–F · 3527 Ų buried · 60 hydrogen bonds · protein-protein
• A–D · 1195 Ų buried · 15 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 covalent (additive adduct).

Compared structures

• 4CBB · APO FORM OF BETAINE ALDEHYDE DEHYDROGENASE FROM Pseudomonas aeruginosa · the same entry in another collection · chain H against H, 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 H 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 Q9HTJ1
• Elsewhere: RCSB PDB 4CBB · PDBe 4CBB · UniProt Q9HTJ1