Zinc in PDB 4o68: Structure of Human Cyclic Gmp-Amp Synthase (Cgas)

All present enzymatic activity of Structure of Human Cyclic Gmp-Amp Synthase (Cgas):
2.7.7.86;

The structure of Structure of Human Cyclic Gmp-Amp Synthase (Cgas), PDB code: 4o68 was solved by X.Zhang, Z.Chen, X.W.Zhang, Z.J.Chen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.67 / 2.44
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	162.194, 47.051, 58.404, 90.00, 90.00, 90.00
R / Rfree (%)	18 / 24.4

The binding sites of Zinc atom in the Structure of Human Cyclic Gmp-Amp Synthase (Cgas) (pdb code 4o68). 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 Human Cyclic Gmp-Amp Synthase (Cgas), PDB code: 4o68:

Zinc binding site 1 out of 1 in the Structure of Human 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 Human Cyclic Gmp-Amp Synthase (Cgas) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn601 b:27.1 occ:1.00 NE2 A:HIS390 2.2 23.0 1.0 SG A:CYS397 2.3 24.1 1.0 SG A:CYS404 2.4 21.6 1.0 SG A:CYS396 2.5 26.7 1.0 CD2 A:HIS390 3.0 21.5 1.0 CE1 A:HIS390 3.2 15.4 1.0 CB A:CYS404 3.3 23.6 1.0 CB A:CYS397 3.4 12.9 1.0 CB A:CYS396 3.6 22.2 1.0 O A:HOH751 3.7 26.0 1.0 N A:CYS404 3.8 24.8 1.0 N A:CYS397 3.8 26.5 1.0 C A:CYS396 3.9 18.6 1.0 CA A:CYS404 4.0 21.7 1.0 CA A:CYS397 4.2 25.4 1.0 CG A:HIS390 4.2 31.7 1.0 ND1 A:HIS390 4.3 27.9 1.0 NH2 A:ARG406 4.3 12.3 1.0 CA A:CYS396 4.3 24.0 1.0 O A:CYS396 4.4 18.0 1.0 O A:GLU402 4.5 48.5 1.0 O A:CYS404 4.5 23.4 1.0 C A:CYS404 4.5 25.3 1.0 O A:HOH716 4.9 25.1 1.0 C A:LYS403 5.0 42.5 1.0

X.Zhang, J.Wu, F.Du, H.Xu, L.Sun, Z.Chen, C.A.Brautigam, X.Zhang, Z.J.Chen. The Cytosolic Dna Sensor Cgas Forms An Oligomeric Complex with Dna and Undergoes Switch-Like Conformational Changes in the Activation Loop. Cell Rep V. 6 421 2014.
ISSN: ESSN 2211-1247
PubMed: 24462292
DOI: 10.1016/J.CELREP.2014.01.003