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Atomistry » Zinc » PDB 4bua-4c09 » 4bvf » |
Zinc in PDB 4bvf: Crystal Structure of Human SIRT3 in Complex with Thioalkylimidate Formed From Thio-Acetyl-Lysine ACS2-Peptide Crystallized in Presence of the Inhibitor Ex-527Enzymatic activity of Crystal Structure of Human SIRT3 in Complex with Thioalkylimidate Formed From Thio-Acetyl-Lysine ACS2-Peptide Crystallized in Presence of the Inhibitor Ex-527
All present enzymatic activity of Crystal Structure of Human SIRT3 in Complex with Thioalkylimidate Formed From Thio-Acetyl-Lysine ACS2-Peptide Crystallized in Presence of the Inhibitor Ex-527:
6.2.1.1; Protein crystallography data
The structure of Crystal Structure of Human SIRT3 in Complex with Thioalkylimidate Formed From Thio-Acetyl-Lysine ACS2-Peptide Crystallized in Presence of the Inhibitor Ex-527, PDB code: 4bvf
was solved by
M.Gertz,
M.Weyand,
C.Steegborn,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of Human SIRT3 in Complex with Thioalkylimidate Formed From Thio-Acetyl-Lysine ACS2-Peptide Crystallized in Presence of the Inhibitor Ex-527
(pdb code 4bvf). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of Human SIRT3 in Complex with Thioalkylimidate Formed From Thio-Acetyl-Lysine ACS2-Peptide Crystallized in Presence of the Inhibitor Ex-527, PDB code: 4bvf: Zinc binding site 1 out of 1 in 4bvfGo back to Zinc Binding Sites List in 4bvf
Zinc binding site 1 out
of 1 in the Crystal Structure of Human SIRT3 in Complex with Thioalkylimidate Formed From Thio-Acetyl-Lysine ACS2-Peptide Crystallized in Presence of the Inhibitor Ex-527
Mono view Stereo pair view
Reference:
M.Gertz,
F.Fischer,
G.T.T.Nguyen,
M.Lakshminarasimhan,
M.Schutkowski,
M.Weyand,
C.Steegborn.
Ex-527 Inhibits Sirtuins By Exploiting Their Unique Nad+-Dependent Deacetylation Mechanism Proc.Natl.Acad.Sci.Usa V. 110 E2772 2013.
Page generated: Wed Dec 16 05:06:22 2020
ISSN: ISSN 0027-8424 PubMed: 23840057 DOI: 10.1073/PNAS.1303628110 |
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