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5G17

Bordetella Alcaligenes HDAH (T101A) bound to 9,9,9-trifluoro-8,8- dihydroxy-N-phenylnonanamide.

Summary for 5G17
Entry DOI10.2210/pdb5g17/pdb
Related5G0X 5G0Y 5G10 5G11 5G12 5G13 5G1A 5G1B 5G1C
DescriptorHISTONE DEACETYLASE-LIKE AMIDOHYDROLASE, ZINC ION, POTASSIUM ION, ... (5 entities in total)
Functional Keywordshydrolase, hdah, hdac, hdlp
Biological sourceALCALIGENES
Total number of polymer chains2
Total formula weight79728.90
Authors
Kraemer, A.,Meyer-Almes, F.J.,Yildiz, O. (deposition date: 2016-03-23, release date: 2017-04-12, Last modification date: 2024-01-10)
Primary citationMeyners, C.,Kramer, A.,Yildiz, O.,Meyer-Almes, F.J.
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.
Biochim. Biophys. Acta, 1861:1855-1863, 2017
Cited by
PubMed: 28389333
DOI: 10.1016/j.bbagen.2017.04.001
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.51 Å)
Structure validation

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