Zinc in PDB 4o69: Human Cyclic Gmp-Amp Synthase (Cgas) in Complex with Sulfate Ion

All present enzymatic activity of Human Cyclic Gmp-Amp Synthase (Cgas) in Complex with Sulfate Ion:
2.7.7.86;

The structure of Human Cyclic Gmp-Amp Synthase (Cgas) in Complex with Sulfate Ion, PDB code: 4o69 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)	33.07 / 2.25
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	101.027, 101.027, 241.331, 90.00, 90.00, 120.00
R / Rfree (%)	19 / 22.4

The binding sites of Zinc atom in the Human Cyclic Gmp-Amp Synthase (Cgas) in Complex with Sulfate Ion (pdb code 4o69). 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 Human Cyclic Gmp-Amp Synthase (Cgas) in Complex with Sulfate Ion, PDB code: 4o69:

Zinc binding site 1 out of 1 in the Human Cyclic Gmp-Amp Synthase (Cgas) in Complex with Sulfate Ion


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Cyclic Gmp-Amp Synthase (Cgas) in Complex with Sulfate Ion within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn601 b:40.2 occ:1.00 NE2 A:HIS390 2.1 41.6 1.0 SG A:CYS396 2.3 37.2 1.0 SG A:CYS397 2.3 41.5 1.0 SG A:CYS404 2.5 36.8 1.0 CD2 A:HIS390 3.0 33.0 1.0 CE1 A:HIS390 3.1 42.5 1.0 CB A:CYS397 3.3 42.8 1.0 CB A:CYS396 3.4 34.5 1.0 CB A:CYS404 3.5 39.2 1.0 N A:CYS397 3.6 39.8 1.0 C A:CYS396 3.7 37.5 1.0 N A:CYS404 3.9 43.1 1.0 O A:HOH815 4.0 36.7 1.0 O A:CYS396 4.0 40.7 1.0 CA A:CYS397 4.0 47.9 1.0 CA A:CYS396 4.1 40.4 1.0 CG A:HIS390 4.2 39.1 1.0 CA A:CYS404 4.2 47.7 1.0 ND1 A:HIS390 4.2 37.4 1.0 O A:GLU402 4.3 44.6 1.0 NH2 A:ARG406 4.3 31.7 1.0 O A:HOH723 4.4 43.9 1.0 O A:HOH718 4.7 42.3 1.0 C A:CYS404 4.8 52.3 1.0 O A:CYS404 4.8 46.0 1.0 O A:HOH725 4.9 53.9 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