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Zinc in PDB 4bve: Crystal Structure of Human SIRT3 in Complex with Thioalkylimidate Formed From Thio-Acetyl-Lysine ACS2- Peptide

Enzymatic 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:

Resolution Low / High (Å) 34.14 / 2.05
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 80.990, 126.970, 76.490, 90.00, 90.00, 90.00
R / Rfree (%) 16.193 / 20.789

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 (Cl) 1 atom

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 (pdb code 4bve). 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, PDB code: 4bve:

Zinc binding site 1 out of 1 in 4bve

Go back to Zinc Binding Sites List in 4bve
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


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 Thioalkylimidate Formed From Thio-Acetyl-Lysine ACS2- Peptide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1395

b:13.7
occ:1.00
 SG A:CYS283 2.2 11.3 1.0
SG A:CYS280 2.3 11.8 1.0
SG A:CYS259 2.4 14.2 1.0
SG A:CYS256 2.4 10.6 1.0
CB A:CYS280 3.0 10.5 1.0
CB A:CYS256 3.1 11.5 1.0
CB A:CYS259 3.4 13.3 1.0
CB A:CYS283 3.4 11.9 1.0
N A:CYS259 3.7 15.4 1.0
N A:CYS283 3.9 13.6 1.0
CG2 A:VAL282 3.9 14.7 0.5
CA A:CYS259 4.1 14.4 1.0
CA A:CYS283 4.1 12.2 1.0
CA A:CYS280 4.5 11.3 1.0
N A:GLY285 4.5 13.1 1.0
CA A:CYS256 4.6 11.0 1.0
C A:CYS283 4.7 12.8 1.0
CB A:VAL282 4.7 15.5 0.5
CB A:VAL258 4.7 11.1 1.0
N A:THR284 4.8 11.2 1.0
CA A:GLY285 4.8 12.2 1.0
C A:CYS259 4.8 16.9 1.0
C A:VAL282 4.9 16.9 1.0
C A:VAL258 4.9 15.5 1.0
CB A:ARG261 5.0 23.6 1.0

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.
ISSN: ISSN 0027-8424
PubMed: 23840057
DOI: 10.1073/PNAS.1303628110
Page generated: Wed Dec 16 05:06:21 2020

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