Atomistry » Zinc » PDB 5g2b-5gk8 » 5g4c
Atomistry »
  Zinc »
    PDB 5g2b-5gk8 »
      5g4c »

Zinc in PDB 5g4c: Human SIRT2 Catalyse Short Chain Fatty Acyl Lysine

Protein crystallography data

The structure of Human SIRT2 Catalyse Short Chain Fatty Acyl Lysine, PDB code: 5g4c was solved by Y.Wang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.00 / 2.10
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 37.341, 117.310, 71.346, 90.00, 92.65, 90.00
R / Rfree (%) 18.3 / 22

Zinc Binding Sites:

The binding sites of Zinc atom in the Human SIRT2 Catalyse Short Chain Fatty Acyl Lysine (pdb code 5g4c). 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 Human SIRT2 Catalyse Short Chain Fatty Acyl Lysine, PDB code: 5g4c:

Zinc binding site 1 out of 1 in 5g4c

Go back to Zinc Binding Sites List in 5g4c
Zinc binding site 1 out of 1 in the Human SIRT2 Catalyse Short Chain Fatty Acyl Lysine


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human SIRT2 Catalyse Short Chain Fatty Acyl Lysine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1356

b:21.6
occ:1.00
SG A:CYS200 2.3 23.1 1.0
SG A:CYS224 2.4 19.2 1.0
SG A:CYS221 2.4 21.4 1.0
SG A:CYS195 2.5 34.4 1.0
CB A:CYS200 3.1 22.3 1.0
CB A:CYS221 3.2 19.1 1.0
CB A:CYS195 3.2 23.0 1.0
CB A:CYS224 3.4 19.5 1.0
N A:CYS224 3.9 25.5 1.0
CB A:HIS202 4.1 20.9 1.0
CA A:CYS224 4.1 25.6 1.0
N A:HIS202 4.4 21.8 1.0
CA A:CYS200 4.5 28.5 1.0
CB A:SER197 4.6 25.8 1.0
N A:ARG201 4.6 22.0 1.0
CA A:CYS221 4.7 25.9 1.0
C A:CYS224 4.7 23.4 1.0
O A:HOH2088 4.7 29.8 1.0
CA A:CYS195 4.7 19.3 1.0
C A:CYS200 4.7 26.1 1.0
CB A:SER226 4.8 18.6 1.0
N A:GLN225 4.8 19.4 1.0
CB A:ASP223 4.8 25.8 1.0
CA A:HIS202 4.9 20.7 1.0
N A:SER226 4.9 21.4 1.0
OG A:SER226 5.0 23.9 1.0

Reference:

J.Jin, B.He, X.Zhang, H.Lin, Y.Wang. SIRT2 Reverses 4-Oxononanoyl Lysine Modification on Histones. J. Am. Chem. Soc. V. 138 12304 2016.
ISSN: ESSN 1520-5126
PubMed: 27610633
DOI: 10.1021/JACS.6B04977
Page generated: Sun Oct 27 16:55:55 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy