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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) |
Authors | Meyners, C. / Kramer, A. / Yildiz, O. / Meyer-Almes, F.J. |
External links | Biochim. Biophys. Acta / PubMed:28389333 |
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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Keywords | HYDROLASE / HDAH / HDAC / HDLP |