5G1B

Bordetella Alcaligenes HDAH native

Summary for 5G1B

Entry DOI	10.2210/pdb5g1b/pdb
Related	5G0X 5G0Y 5G10 5G11 5G12 5G13 5G17 5G1A 5G1C
Descriptor	HISTONE DEACETYLASE-LIKE AMIDOHYDROLASE, ZINC ION, POTASSIUM ION, ... (6 entities in total)
Functional Keywords	hydrolase, hdah, hdac, hdlp
Biological source	ALCALIGENES
Total number of polymer chains	2
Total formula weight	80816.17
Authors	Kraemer, A.,Meyer-Almes, F.J.,Yildiz, O. (deposition date: 2016-03-24, 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 Cited by PubMed: 28389333 DOI: 10.1016/j.bbagen.2017.04.001 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.7 Å)

Structure validation