5G17

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

Summary for 5G17

• Entry DOI: 10.2210/pdb5g17/pdb
• Related: 5G0X 5G0Y 5G10 5G11 5G12 5G13 5G1A 5G1B 5G1C
• Descriptor: HISTONE DEACETYLASE-LIKE AMIDOHYDROLASE, ZINC ION, POTASSIUM ION, ... (5 entities in total)
• Functional Keywords: hydrolase, hdah, hdac, hdlp
• Biological source: ALCALIGENES
• Total number of polymer chains: 2
• Total formula weight: 79728.90

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 citation

Meyners, 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

PubMed Abstract: The analysis of the thermodynamic driving forces of ligand-protein binding has been suggested to be a key component for the selection and optimization of active compounds into drug candidates. The binding enthalpy as deduced from isothermal titration calorimetry (ITC) is usually interpreted assuming single-step binding of a ligand to one conformation of the target protein. Although successful in many cases, these assumptions are oversimplified approximations of the reality with flexible proteins and complicated binding mechanism in many if not most cases. The relationship between protein flexibility and thermodynamic signature of ligand binding is largely understudied.

PubMed: 28389333
DOI: 10.1016/j.bbagen.2017.04.001

Experimental method

X-RAY DIFFRACTION (1.51 Å)