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 Cited by PubMed: 28389333DOI: 10.1016/j.bbagen.2017.04.001 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.42 Å) |
Structure validation
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