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Zinc in PDB 4lew: Structure of Human Cgas

Protein crystallography data

The structure of Structure of Human Cgas, PDB code: 4lew was solved by P.Li, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.75 / 2.04
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 46.815, 111.480, 76.414, 90.00, 92.73, 90.00
R / Rfree (%) 17.9 / 22.3

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of Human Cgas (pdb code 4lew). 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 Human Cgas, PDB code: 4lew:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 4lew

Go back to Zinc Binding Sites List in 4lew
Zinc binding site 1 out of 2 in the Structure of Human Cgas


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Human Cgas within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn601

b:23.8
occ:1.00
NE2 B:HIS390 2.1 23.7 1.0
SG B:CYS396 2.3 23.7 1.0
SG B:CYS397 2.3 23.1 1.0
SG B:CYS404 2.4 21.6 1.0
CD2 B:HIS390 3.0 19.1 1.0
CE1 B:HIS390 3.2 23.1 1.0
CB B:CYS397 3.4 29.8 1.0
CB B:CYS404 3.5 21.4 1.0
CB B:CYS396 3.5 17.9 1.0
N B:CYS397 3.7 19.6 1.0
C B:CYS396 3.7 22.4 1.0
O B:HOH712 3.8 21.9 1.0
N B:CYS404 3.9 27.2 1.0
CA B:CYS397 4.1 24.2 1.0
O B:CYS396 4.2 21.6 1.0
CA B:CYS404 4.2 26.6 1.0
CA B:CYS396 4.2 20.0 1.0
CG B:HIS390 4.2 21.3 1.0
O B:GLU402 4.2 29.3 1.0
ND1 B:HIS390 4.3 22.1 1.0
O B:HOH749 4.4 34.7 1.0
NH1 B:ARG406 4.4 21.2 1.0
O B:HOH725 4.7 29.9 1.0
O B:HOH717 4.7 25.3 1.0
C B:CYS404 4.7 24.0 1.0
O B:CYS404 4.8 26.4 1.0

Zinc binding site 2 out of 2 in 4lew

Go back to Zinc Binding Sites List in 4lew
Zinc binding site 2 out of 2 in the Structure of Human Cgas


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of Human Cgas within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn601

b:20.3
occ:1.00
NE2 A:HIS390 2.1 21.3 1.0
SG A:CYS396 2.3 21.1 1.0
SG A:CYS397 2.3 21.8 1.0
SG A:CYS404 2.3 19.0 1.0
CD2 A:HIS390 3.0 17.2 1.0
CE1 A:HIS390 3.2 18.8 1.0
CB A:CYS397 3.4 22.5 1.0
CB A:CYS404 3.4 20.1 1.0
CB A:CYS396 3.5 22.2 1.0
N A:CYS397 3.7 22.7 1.0
C A:CYS396 3.8 21.5 1.0
N A:CYS404 3.9 22.7 1.0
O A:HOH704 3.9 21.1 1.0
CA A:CYS397 4.1 23.6 1.0
CA A:CYS404 4.1 21.7 1.0
CA A:CYS396 4.2 23.9 1.0
CG A:HIS390 4.2 18.8 1.0
ND1 A:HIS390 4.2 19.6 1.0
O A:CYS396 4.2 21.2 1.0
O A:GLU402 4.4 33.0 1.0
O A:HOH748 4.4 31.2 1.0
NH1 A:ARG406 4.4 16.2 1.0
O A:HOH757 4.6 27.7 1.0
C A:CYS404 4.7 21.8 1.0
O A:HOH725 4.7 26.1 1.0
O A:CYS404 4.8 22.6 1.0

Reference:

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
Page generated: Wed Dec 16 05:32:00 2020

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