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Atomistry » Chlorine » PDB 4brl-4c00 » 4bve | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 4brl-4c00 » 4bve » |
Chlorine in PDB 4bve: Crystal Structure of Human SIRT3 in Complex with Thioalkylimidate Formed From Thio-Acetyl-Lysine ACS2- PeptideEnzymatic activity of Crystal Structure of Human SIRT3 in Complex with Thioalkylimidate Formed From Thio-Acetyl-Lysine ACS2- Peptide
All present enzymatic activity of Crystal Structure of Human SIRT3 in Complex with Thioalkylimidate Formed From Thio-Acetyl-Lysine ACS2- Peptide:
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, PDB code: 4bve
was solved by
M.Gertz,
M.Weyand,
C.Steegborn,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 4bve:
The structure of Crystal Structure of Human SIRT3 in Complex with Thioalkylimidate Formed From Thio-Acetyl-Lysine ACS2- Peptide also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure of Human SIRT3 in Complex with Thioalkylimidate Formed From Thio-Acetyl-Lysine ACS2- Peptide
(pdb code 4bve). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of Human SIRT3 in Complex with Thioalkylimidate Formed From Thio-Acetyl-Lysine ACS2- Peptide, PDB code: 4bve: Chlorine binding site 1 out of 1 in 4bveGo back to![]() ![]()
Chlorine binding site 1 out
of 1 in the Crystal Structure of Human SIRT3 in Complex with Thioalkylimidate Formed From Thio-Acetyl-Lysine ACS2- Peptide
![]() 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: Fri Jul 11 13:37:13 2025
ISSN: ISSN 0027-8424 PubMed: 23840057 DOI: 10.1073/PNAS.1303628110 |
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