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Zinc in PDB 4bvg: Crystal Structure of Human SIRT3 in Complex with Native Alkylimidate Formed From Acetyl-Lysine ACS2-Peptide Crystallized in Presence of the Inhibitor Ex-527

Enzymatic activity of Crystal Structure of Human SIRT3 in Complex with Native Alkylimidate Formed From 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 Native Alkylimidate Formed From 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 Native Alkylimidate Formed From Acetyl-Lysine ACS2-Peptide Crystallized in Presence of the Inhibitor Ex-527, PDB code: 4bvg was solved by G.T.T.Nguyen, M.Gertz, M.Weyand, C.Steegborn, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.18 / 2.50
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 78.023, 131.329, 76.508, 90.00, 90.00, 90.00
R / Rfree (%) 18.2 / 24.8

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Human SIRT3 in Complex with Native Alkylimidate Formed From Acetyl-Lysine ACS2-Peptide Crystallized in Presence of the Inhibitor Ex-527 (pdb code 4bvg). 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 Native Alkylimidate Formed From Acetyl-Lysine ACS2-Peptide Crystallized in Presence of the Inhibitor Ex-527, PDB code: 4bvg:

Zinc binding site 1 out of 1 in 4bvg

Go back to Zinc Binding Sites List in 4bvg
Zinc binding site 1 out of 1 in the Crystal Structure of Human SIRT3 in Complex with Native Alkylimidate Formed From Acetyl-Lysine ACS2-Peptide Crystallized in Presence of the Inhibitor Ex-527


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Human SIRT3 in Complex with Native Alkylimidate Formed From Acetyl-Lysine ACS2-Peptide Crystallized in Presence of the Inhibitor Ex-527 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1409

b:28.3
occ:1.00
 SG A:CYS259 2.1 26.3 1.0
SG A:CYS280 2.2 28.9 1.0
SG A:CYS283 2.3 30.7 1.0
SG A:CYS256 2.4 28.4 1.0
CB A:CYS280 3.0 27.5 1.0
CB A:CYS259 3.2 29.3 1.0
CB A:CYS256 3.3 22.6 1.0
CB A:CYS283 3.4 30.9 1.0
N A:CYS259 3.8 30.5 1.0
N A:CYS283 3.8 25.3 1.0
CA A:CYS283 4.1 27.1 1.0
CA A:CYS259 4.1 31.4 1.0
CA A:CYS280 4.4 27.5 1.0
C A:CYS283 4.7 27.7 1.0
N A:GLY285 4.7 28.6 1.0
CB A:VAL258 4.7 28.7 1.0
CA A:CYS256 4.7 23.1 1.0
C A:CYS259 4.8 31.1 1.0
N A:THR284 4.8 27.7 1.0
C A:VAL258 4.9 30.6 1.0
C A:VAL282 4.9 27.6 1.0
CB A:VAL282 5.0 22.3 1.0
N A:GLN260 5.0 31.3 1.0

Reference:

M.Gertz, F.Fischer, G.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. V. 110 E2772 2013U.S.A..
ISSN: ESSN 1091-6490
PubMed: 23840057
DOI: 10.1073/PNAS.1303628110
Page generated: Wed Aug 20 16:23:40 2025

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