Zinc in PDB 4lez: Structure of Mouse Cgas Bound to An 18BP Dna and Cgas Product

The structure of Structure of Mouse Cgas Bound to An 18BP Dna and Cgas Product, PDB code: 4lez was solved by P.Li, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.55 / 2.36
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	79.209, 99.031, 142.631, 90.00, 90.00, 90.00
R / Rfree (%)	19.2 / 24.7

The binding sites of Zinc atom in the Structure of Mouse Cgas Bound to An 18BP Dna and Cgas Product (pdb code 4lez). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structure of Mouse Cgas Bound to An 18BP Dna and Cgas Product, PDB code: 4lez:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Structure of Mouse Cgas Bound to An 18BP Dna and Cgas Product


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Mouse Cgas Bound to An 18BP Dna and Cgas Product within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn601 b:44.6 occ:1.00 NE2 A:HIS378 2.1 43.5 1.0 SG A:CYS384 2.3 42.1 1.0 SG A:CYS385 2.3 39.1 1.0 SG A:CYS392 2.5 41.0 1.0 CD2 A:HIS378 2.9 36.7 1.0 CE1 A:HIS378 3.2 41.1 1.0 CB A:CYS385 3.3 34.0 1.0 CB A:CYS392 3.4 35.6 1.0 N A:CYS385 3.6 42.5 1.0 CB A:CYS384 3.6 33.7 1.0 N A:CYS392 3.7 47.2 1.0 C A:CYS384 3.7 42.2 1.0 CA A:CYS385 4.0 42.3 1.0 CA A:CYS392 4.1 43.6 1.0 CG A:HIS378 4.1 41.1 1.0 CA A:CYS384 4.2 39.4 1.0 ND1 A:HIS378 4.2 39.7 1.0 O A:CYS384 4.2 42.6 1.0 NH1 A:ARG394 4.3 34.7 1.0 C A:CYS392 4.6 45.8 1.0 O A:ALA390 4.7 49.4 1.0 O A:CYS392 4.7 47.0 1.0 C A:LYS391 4.7 46.6 1.0 O A:HOH742 4.9 44.2 1.0

Zinc binding site 2 out of 2 in the Structure of Mouse Cgas Bound to An 18BP Dna and Cgas Product


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of Mouse Cgas Bound to An 18BP Dna and Cgas Product within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn601 b:43.0 occ:1.00 NE2 C:HIS378 2.1 38.6 1.0 SG C:CYS384 2.3 40.8 1.0 SG C:CYS385 2.3 39.9 1.0 SG C:CYS392 2.4 38.0 1.0 CD2 C:HIS378 3.0 30.9 1.0 CE1 C:HIS378 3.2 41.1 1.0 CB C:CYS392 3.4 33.6 1.0 CB C:CYS385 3.4 34.9 1.0 CB C:CYS384 3.5 40.3 1.0 N C:CYS385 3.6 35.4 1.0 C C:CYS384 3.7 40.2 1.0 N C:CYS392 3.7 41.5 1.0 O C:CYS384 4.0 38.2 1.0 CA C:CYS384 4.1 42.7 1.0 CA C:CYS392 4.1 40.0 1.0 CA C:CYS385 4.1 36.2 1.0 CG C:HIS378 4.2 31.9 1.0 O C:HOH703 4.2 38.1 1.0 ND1 C:HIS378 4.3 32.7 1.0 NH1 C:ARG394 4.3 37.6 1.0 C C:CYS392 4.7 38.8 1.0 C C:LYS391 4.7 45.0 1.0 O C:ALA390 4.7 42.6 1.0 O C:CYS392 4.7 51.4 1.0 O C:HOH713 4.8 44.3 1.0

X.Li, C.Shu, G.Yi, C.T.Chaton, C.L.Shelton, J.Diao, X.Zuo, C.C.Kao, A.B.Herr, P.Li. Cyclic Gmp-Amp Synthase Is Activated By Double-Stranded Dna-Induced Oligomerization. Immunity V. 39 1019 2013.
ISSN: ISSN 1074-7613
PubMed: 24332030
DOI: 10.1016/J.IMMUNI.2013.10.019