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-Structure paper
Title | The thermodynamic signature of ligand binding to histone deacetylase-like amidohydrolases is most sensitive to the flexibility in the L2-loop lining the active site pocket. |
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Journal, issue, pages | Biochim. Biophys. Acta, Vol. 1861, Page 1855-1863, Year 2017 |
Publish date | Mar 23, 2016 (structure data deposition date) |
![]() | Meyners, C. / Kramer, A. / Yildiz, O. / Meyer-Almes, F.J. |
![]() | ![]() ![]() |
Methods | X-ray diffraction |
Resolution | 1.42 - 1.7 Å |
Structure data | ![]() PDB-5g17: ![]() PDB-5g1a: ![]() PDB-5g1b: |
Chemicals | ![]() ChemComp-ZN: ![]() ChemComp-K: ![]() ChemComp-6DK: ![]() ChemComp-HOH: ![]() ChemComp-7H1: ![]() ChemComp-1PE: ![]() ChemComp-PEG: |
Source |
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![]() | HYDROLASE / HDAH / HDAC / HDLP |