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-Structure paper
Title | Histidine-51 facilitates deprotonation of the zinc-bound ligand during catalysis by horse liver alcohol dehydrogenase |
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Journal, issue, pages | To Be Published |
Publish date | Feb 5, 2023 (structure data deposition date) |
![]() | Plapp, B.V. / Kovaleva, E.G. |
![]() | Search PubMed |
Methods | X-ray diffraction |
Resolution | 1.2 - 1.47 Å |
Structure data | ![]() PDB-8g2l: ![]() PDB-8g2s: ![]() PDB-8g2x: ![]() PDB-8g39: ![]() PDB-8g4v: |
Chemicals | ![]() ChemComp-ZN: ![]() ChemComp-NAJ: ![]() ChemComp-ETF: ![]() ChemComp-MPD: ![]() ChemComp-MRD: ![]() ChemComp-HOH: ![]() ChemComp-DKA: ![]() ChemComp-PZO: ![]() ChemComp-NAI: ![]() ChemComp-CXF: ![]() ChemComp-PFB: |
Source |
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![]() | OXIDOREDUCTASE / alcohol dehydrogenase horse liver His-48 Gln substitution complex with NAD+ and trifluoroethanol / alcohol dehydrogenase horse liver His-51 Gln substitution complex with NAD+ and capric acid / alcohol dehydrogenase horse liver His-48 Gln substitution complex with NAD+ and pyrazole / alcohol dehydrogenase horse liver His-51-Gln substitution complex with NADH and N-cyclohexylformamide / alcohol dehydrogenase horse liver His-51- Gln substitution / complex with NAD+ and pentafluorobenzyl alcohol |