Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-294 of T. brockii ADH by E. histolytica ADH

Structure

x-ray diffraction · resolution 1.4 · 1 distinct chain · 30% helix, 27% strand (DSSP).

Ligands and binding sites

• ZN · Zinc ion · metal · 4 copies · chains A, B, C, D
• NA · Sodium ion · metal · 2 copies · chains C, D
• NO3 · Nitrate ion · ion · 2 copies · chains A, B, C, D
• OXY · Oxygen molecule · ion · chains A, C
• EDO · 1,2-ethanediol · additive · 14 copies · chains B, D, C, A
• CAC · Cacodylate ion · additive · 4 copies · chains A, C, B, D
• IMD · Imidazole · additive · chains C, D

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

Pockets

11 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

Interfaces

6 interfaces between chains.

• A–C · 1979 Ų buried · 43 hydrogen bonds · protein-protein
• B–D · 1974 Ų buried · 42 hydrogen bonds · protein-protein
• B–C · 1077 Ų buried · 21 hydrogen bonds · protein-protein
• A–D · 1039 Ų buried · 20 hydrogen bonds · protein-protein
• A–B · 717 Ų buried · 10 hydrogen bonds · protein-protein

Compared structures

• 3FPC · Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-294… · the same entry in another collection · chain C against C, TM-score 1.00
• P14941 · AlphaFold monomer V2.0 prediction for NADP-dependent isopropanol dehydrogenase (P14941) · a predicted model of the same protein · chain D against A, TM-score 1.00
• P35630 · AlphaFold monomer V2.0 prediction for NADP-dependent isopropanol dehydrogenase (P35630) · a predicted model of the same protein · chain B 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 P14941
• Every structure of UniProt P35630
• Elsewhere: RCSB PDB 3FPC · PDBe 3FPC · UniProt P14941 · UniProt P35630