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Zinc in PDB 4jlx: Structure of Porcine Cyclic Gmp-Amp Synthase (Cgas)

Protein crystallography data

The structure of Structure of Porcine Cyclic Gmp-Amp Synthase (Cgas), PDB code: 4jlx was solved by F.Civril, K.P.Hopfner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.46 / 2.00
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 47.402, 118.014, 142.599, 90.00, 90.00, 90.00
R / Rfree (%) 18.8 / 21.5

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of Porcine Cyclic Gmp-Amp Synthase (Cgas) (pdb code 4jlx). 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 Structure of Porcine Cyclic Gmp-Amp Synthase (Cgas), PDB code: 4jlx:

Zinc binding site 1 out of 1 in 4jlx

Go back to Zinc Binding Sites List in 4jlx
Zinc binding site 1 out of 1 in the Structure of Porcine Cyclic Gmp-Amp Synthase (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 Porcine Cyclic Gmp-Amp Synthase (Cgas) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn501

b:31.0
occ:1.00
NE2 A:HIS367 2.1 33.4 1.0
SG A:CYS373 2.3 30.2 1.0
SG A:CYS374 2.3 28.0 1.0
SG A:CYS381 2.4 27.1 1.0
CD2 A:HIS367 2.9 22.7 1.0
CE1 A:HIS367 3.2 34.1 1.0
CB A:CYS374 3.3 29.6 1.0
CB A:CYS381 3.4 23.9 1.0
CB A:CYS373 3.6 26.8 1.0
N A:CYS374 3.8 29.3 1.0
C A:CYS373 3.8 24.5 1.0
N A:CYS381 3.8 31.5 1.0
O A:HOH665 3.9 32.6 1.0
O A:CYS373 4.1 26.7 1.0
CA A:CYS381 4.1 28.4 1.0
CA A:CYS374 4.1 30.6 1.0
CG A:HIS367 4.1 29.1 1.0
CA A:CYS373 4.2 32.8 1.0
ND1 A:HIS367 4.2 31.4 1.0
NH1 A:ARG383 4.5 28.2 1.0
C A:CYS381 4.6 29.1 1.0
O A:HOH603 4.6 31.7 1.0
O A:CYS381 4.6 26.4 1.0
O A:HOH691 4.8 38.4 1.0
C A:LYS380 4.9 27.5 1.0

Reference:

F.Civril, T.Deimling, C.C.O.Mann, A.Ablasser, M.Moldt, G.Witte, V.Hornung, K.P.Hopfner. Structural Mechanism of Cytosolic Dna Sensing By Cgas Nature V. 498 332 2013.
ISSN: ISSN 0028-0836
PubMed: 23722159
DOI: 10.1038/NATURE12305
Page generated: Sun Oct 27 01:21:46 2024

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