5G1A

Bordetella Alcaligenes HDAH bound to PFSAHA

Summary for 5G1A

• Entry DOI: 10.2210/pdb5g1a/pdb
• Related: 5G0X 5G0Y 5G10 5G11 5G12 5G13 5G17 5G1B 5G1C
• Descriptor: HISTONE DEACETYLASE-LIKE AMIDOHYDROLASE, ZINC ION, POTASSIUM ION, ... (7 entities in total)
• Functional Keywords: hydrolase, hdah, hdac, hdlp
• Biological source: ALCALIGENES
• Total number of polymer chains: 2
• Total formula weight: 81988.83

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

Experimental method

X-RAY DIFFRACTION (1.42 Å)