4bvh Summary

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CRYSTAL STRUCTURE OF HUMAN SIRT3 IN COMPLEX WITH THE INHIBITOR EX-527 AND 2'-O-ACETYL-ADP-RIBOSE

The structure was published by Gertz, M., Fischer, F., Nguyen, G.T.T., et al., Schutkowski, M., Weyand, M., and Steegborn, C., in 2013 in a paper entitled "Ex-527 Inhibits Sirtuins by Exploiting Their Unique Nad+-Dependent Deacetylation Mechanism" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.9 Å and deposited in 2013.

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

This PDB entry contains multiple copies of the structure of NAD-DEPENDENT PROTEIN DEACETYLASE SIRTUIN-3, MITOCHONDRIAL.

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 PROTEIN DEACETYLASE SIRTUIN-3, MITOCHONDRIAL Q9NTG7 (116-399) (SIR3_HUMAN)search Homo sapienssearch < 90% 284 95%
B NAD-DEPENDENT PROTEIN DEACETYLASE SIRTUIN-3, MITOCHONDRIAL Q9NTG7 (116-399) (SIR3_HUMAN)search Homo sapienssearch < 90% 284 95%
C NAD-DEPENDENT PROTEIN DEACETYLASE SIRTUIN-3, MITOCHONDRIAL Q9NTG7 (116-399) (SIR3_HUMAN)search Homo sapienssearch < 90% 284 95%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q9NTG7 (116 - 399) NAD-DEPENDENT PROTEIN DEACETYLASE SIRTUIN-3, MITOCHONDRIAL Homo sapiens

Chain Sequence family (Pfam)
A, B, C Sir2 familysearch

Chain ID Molecular function (GO) Biological process (GO)
A, B, C (Q9NTG7) NAD+ bindingsearch zinc ion bindingsearch NAD bindingsearch hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidessearch protein deacetylationsearch

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