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 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy