Zinc in PDB 6x5a: The Mouse Cgas Catalytic Domain Binding to Human Nucleosome That Purified From HEK293T Cells

Enzymatic activity of The Mouse Cgas Catalytic Domain Binding to Human Nucleosome That Purified From HEK293T Cells

All present enzymatic activity of The Mouse Cgas Catalytic Domain Binding to Human Nucleosome That Purified From HEK293T Cells:
2.7.7.86;

Zinc Binding Sites:

The binding sites of Zinc atom in the The Mouse Cgas Catalytic Domain Binding to Human Nucleosome That Purified From HEK293T Cells (pdb code 6x5a). 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 The Mouse Cgas Catalytic Domain Binding to Human Nucleosome That Purified From HEK293T Cells, PDB code: 6x5a:

Zinc binding site 1 out of 1 in 6x5a

Go back to Zinc Binding Sites List in 6x5a
Zinc binding site 1 out of 1 in the The Mouse Cgas Catalytic Domain Binding to Human Nucleosome That Purified From HEK293T Cells


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Mouse Cgas Catalytic Domain Binding to Human Nucleosome That Purified From HEK293T Cells within 5.0Å range:
probe atom residue distance (Å) B Occ
K:Zn601

b:0.4
occ:1.01
NE2 K:HIS378 2.6 0.9 1.0
SG K:CYS392 3.2 1.0 1.0
CE1 K:HIS378 3.2 0.9 1.0
CD K:LYS395 3.4 1.0 1.0
CD2 K:HIS378 3.6 0.9 1.0
CG K:LYS395 3.7 1.0 1.0
SG K:CYS385 3.8 0.1 1.0
O K:CYS392 3.8 1.0 1.0
N K:CYS385 4.1 0.1 1.0
N K:CYS392 4.1 1.0 1.0
CB K:LYS395 4.3 1.0 1.0
C K:CYS392 4.3 1.0 1.0
CA K:CYS385 4.3 0.1 1.0
N K:LYS395 4.4 1.0 1.0
OE1 K:GLU396 4.4 1.0 1.0
ND1 K:HIS378 4.4 0.9 1.0
CB K:CYS392 4.5 1.0 1.0
CA K:CYS392 4.6 1.0 1.0
CB K:CYS385 4.6 0.1 1.0
CG K:HIS378 4.6 0.9 1.0
NZ K:LYS391 4.8 0.7 1.0
CE K:LYS395 4.8 1.0 1.0
CB K:CYS384 4.8 0.9 1.0
N K:ARG394 4.9 1.0 1.0
OE2 K:GLU396 5.0 1.0 1.0

Reference:

B.Zhao, P.Xu, C.M.Rowlett, T.Jing, O.Shinde, Y.Lei, A.P.West, W.R.Liu, P.Li. The Molecular Basis of Tight Nuclear Tethering and Inactivation of Cgas. Nature V. 587 673 2020.
ISSN: ESSN 1476-4687
PubMed: 32911481
DOI: 10.1038/S41586-020-2749-Z
Page generated: Wed Dec 16 13:08:34 2020

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