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2QQG

Hst2 bound to ADP-HPD, acetyllated histone H4 and nicotinamide

Summary for 2QQG
Entry DOI10.2210/pdb2qqg/pdb
Related2OD9
DescriptorNAD-dependent deacetylase HST2, Histone H4, ZINC ION, ... (6 entities in total)
Functional Keywordshst2, sir2, histone deacetylase, hydrolase, metal-binding, nad, nucleus, repressor, transcription, transcription regulation, zinc
Biological sourceSaccharomyces cerevisiae (baker's yeast)
More
Cellular locationCytoplasm: P53686
Nucleus: P02309
Total number of polymer chains2
Total formula weight36835.31
Authors
Marmorstein, R.,Sanders, B.,Zhao, K.,Slama, J. (deposition date: 2007-07-26, release date: 2007-10-09, Last modification date: 2023-11-15)
Primary citationSanders, B.D.,Zhao, K.,Slama, J.T.,Marmorstein, R.
Structural basis for nicotinamide inhibition and base exchange in sir2 enzymes.
Mol.Cell, 25:463-472, 2007
Cited by
PubMed: 17289592
DOI: 10.1016/j.molcel.2006.12.022
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.05 Å)
Structure validation

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