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Structure paper

TitleThe 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.
Journal, issue, pagesBiochim. Biophys. Acta, Vol. 1861, Page 1855-1863, Year 2017
Publish dateMar 23, 2016 (structure data deposition date)
AuthorsMeyners, C. / Kramer, A. / Yildiz, O. / Meyer-Almes, F.J.
External linksBiochim. Biophys. Acta / PubMed:28389333
MethodsX-ray diffraction
Resolution1.42 - 1.7 Å
Structure data

PDB-5g17:
Bordetella Alcaligenes HDAH (T101A) bound to 9,9,9-trifluoro-8,8- dihydroxy-N-phenylnonanamide.
Method: X-RAY DIFFRACTION / Resolution: 1.51 Å

PDB-5g1a:
Bordetella Alcaligenes HDAH bound to PFSAHA
Method: X-RAY DIFFRACTION / Resolution: 1.42 Å

PDB-5g1b:
Bordetella Alcaligenes HDAH native
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-K:
Unknown entry

ChemComp-6DK:
9,9,9-tris(fluoranyl)-8,8-bis(oxidanyl)-~{N}-phenyl-nonanamide

ChemComp-HOH:
WATER

ChemComp-7H1:
2,2,3,3,4,4,5,5,6,6,7,7-dodecakis(fluoranyl)-~{N}-oxidanyl-~{N}'-phenyl-octanediamide

ChemComp-1PE:
PENTAETHYLENE GLYCOL / precipitant*YM

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

Source
  • alcaligenes (bacteria)
KeywordsHYDROLASE / HDAH / HDAC / HDLP

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