Q165E/S254K double mutant chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-295 of T. brockii adh by C. beijerinckii adh

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 27% strand (DSSP).

Ligands and binding sites

• ZN · Zinc ion · metal · 4 copies · chains A, B, C, D
• CL · Chloride ion · ion · 6 copies · chains A, D, B, C
• EDO · 1,2-ethanediol · additive · 11 copies · chains A, C, B
• ACT · Acetate ion · additive · 4 copies · chains A, C, B, D

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

Pockets

15 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

Interfaces

6 interfaces between chains.

• A–C · 1964 Ų buried · 37 hydrogen bonds · protein-protein
• B–D · 1943 Ų buried · 39 hydrogen bonds · protein-protein
• C–D · 1174 Ų buried · 24 hydrogen bonds · protein-protein
• A–B · 1172 Ų buried · 28 hydrogen bonds · protein-protein
• A–D · 736 Ų buried · 8 hydrogen bonds · protein-protein

Compared structures

• 3FTN · Q165E/S254K Double Mutant Chimera of alcohol dehydrogenase by exchange of the cofactor… · the same entry in another collection · chain A against A, TM-score 1.00
• P14941 · AlphaFold monomer V2.0 prediction for NADP-dependent isopropanol dehydrogenase (P14941) · a predicted model of the same protein · chain A against A, TM-score 1.00
• P25984 · AlphaFold monomer V2.0 prediction for NADP-dependent isopropanol dehydrogenase (P25984) · 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 P14941
• Every structure of UniProt P25984
• Elsewhere: RCSB PDB 3FTN · PDBe 3FTN · UniProt P14941 · UniProt P25984