1szd Summary

pdbe.org/1szd
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Structural basis for nicotinamide cleavage and ADP-ribose transfer by NAD+-dependent Sir2 histone/protein deacetylases

The structure was published by Zhao, K., Harshaw, R., Chai, X., and Marmorstein, R., in 2004 in a paper entitled "Structural basis for nicotinamide cleavage and ADP-ribose transfer by NAD(+)-dependent Sir2 histone/protein deacetylases." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.5 Å and deposited in 2004.

The experimental data on which the structure is based was also deposited.

This PDB entry contains a complex of 2 biomacromolecules, namely NAD-dependent deacetylase HST2 and Histone H4 peptide.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule has more than one probable quaternary state observed. For more details see the quaternary structure page.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A NAD-dependent deacetylase HST2 P53686 (1-294) (HST2_YEAST)search Saccharomyces cerevisiae S288csearch 100% 297 97%
B Histone H4 peptide P02309 (13-22) (H4_YEAST)search Saccharomyces cerevisiae S288csearch 99% 10 80%


This entry contains 2 unique UniProt proteins:

UniProt accession Name Organism PDB
P53686 (1 - 294) NAD-dependent deacetylase HST2 Saccharomyces cerevisiae
P02309 (13 - 22) Histone H4 peptide

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P53686) Sir2 family of transcriptional regulatorssearch TPP-binding domainsearch, SIR2/SIRT2 'Small Domain'search PF02146: Sir2 familysearch
B (P02309)

Chain ID Biological process (GO) Molecular function (GO)
A (P53686) protein deacetylationsearch zinc ion bindingsearch hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidessearch NAD bindingsearch NAD+ bindingsearch

Chain InterPro annotation
A Sirtuin familysearch Sirtuin, class Isearch Sirtuin family, catalytic core domainsearch Sirtuin family, catalytic core small domainsearch DHS-like NAD/FAD-binding domainsearch
B