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Zinc in PDB 4lev: Structure of Human Cgas

Protein crystallography data

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

Resolution Low / High (Å) 38.45 / 1.95
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 212.981, 47.715, 86.869, 90.00, 113.89, 90.00
R / Rfree (%) 16.7 / 20.2

Zinc Binding Sites:

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

Zinc binding site 1 out of 2 in 4lev

Go back to Zinc Binding Sites List in 4lev
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
A:Zn601

b:23.3
occ:1.00
NE2 A:HIS390 2.1 24.1 1.0
SG A:CYS396 2.3 21.3 1.0
SG A:CYS397 2.3 21.8 1.0
SG A:CYS404 2.4 19.6 1.0
CD2 A:HIS390 3.0 18.2 1.0
CE1 A:HIS390 3.3 20.9 1.0
CB A:CYS397 3.3 24.5 1.0
CB A:CYS404 3.4 22.0 1.0
CB A:CYS396 3.5 22.9 1.0
N A:CYS397 3.7 16.2 1.0
C A:CYS396 3.8 20.8 1.0
O A:HOH706 3.9 24.0 1.0
N A:CYS404 3.9 21.1 1.0
CA A:CYS397 4.0 18.6 1.0
CA A:CYS404 4.1 24.0 1.0
CA A:CYS396 4.2 22.6 1.0
CG A:HIS390 4.2 19.6 1.0
O A:CYS396 4.2 20.2 1.0
ND1 A:HIS390 4.3 23.0 1.0
O A:GLU402 4.4 30.2 1.0
NH1 A:ARG406 4.4 17.7 1.0
O A:HOH743 4.5 30.0 1.0
O A:CYS404 4.6 22.1 1.0
C A:CYS404 4.6 22.2 1.0
O A:HOH727 4.8 24.8 1.0
O A:HOH720 4.9 28.9 1.0

Zinc binding site 2 out of 2 in 4lev

Go back to Zinc Binding Sites List in 4lev
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
B:Zn601

b:20.6
occ:1.00
NE2 B:HIS390 2.1 19.6 1.0
SG B:CYS397 2.2 22.6 1.0
SG B:CYS396 2.3 21.9 1.0
SG B:CYS404 2.3 19.9 1.0
CD2 B:HIS390 2.9 16.7 1.0
CE1 B:HIS390 3.2 22.9 1.0
CB B:CYS397 3.3 23.6 1.0
CB B:CYS404 3.4 20.6 1.0
CB B:CYS396 3.5 22.4 1.0
N B:CYS397 3.7 19.2 1.0
C B:CYS396 3.8 23.8 1.0
O B:HOH704 3.9 24.0 1.0
N B:CYS404 3.9 23.3 1.0
CA B:CYS397 4.1 19.9 1.0
CG B:HIS390 4.1 20.2 1.0
CA B:CYS404 4.1 23.6 1.0
O B:CYS396 4.2 24.6 1.0
CA B:CYS396 4.2 23.1 1.0
ND1 B:HIS390 4.2 19.8 1.0
O B:GLU402 4.4 28.7 1.0
NH1 B:ARG406 4.4 16.7 1.0
O B:HOH740 4.5 28.9 1.0
C B:CYS404 4.6 23.9 1.0
O B:CYS404 4.6 21.6 1.0
O B:HOH723 4.7 31.0 1.0
O B:HOH721 4.9 24.3 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: Sun Oct 27 01:47:33 2024

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