Zinc in PDB 5vdo: Human Cyclic Gmp-Amp Synthase (Cgas) in Complex with 2',2'-Cgamp

All present enzymatic activity of Human Cyclic Gmp-Amp Synthase (Cgas) in Complex with 2',2'-Cgamp:
2.7.7.86;

The structure of Human Cyclic Gmp-Amp Synthase (Cgas) in Complex with 2',2'-Cgamp, PDB code: 5vdo was solved by L.J.Byrnes, J.D.Hall, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	55.72 / 3.22
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	216.423, 47.670, 88.861, 90.00, 110.18, 90.00
R / Rfree (%)	20.6 / 25.8

The binding sites of Zinc atom in the Human Cyclic Gmp-Amp Synthase (Cgas) in Complex with 2',2'-Cgamp (pdb code 5vdo). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Human Cyclic Gmp-Amp Synthase (Cgas) in Complex with 2',2'-Cgamp, PDB code: 5vdo:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Human Cyclic Gmp-Amp Synthase (Cgas) in Complex with 2',2'-Cgamp


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 2',2'-Cgamp within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn601 b:74.7 occ:1.00 NE2 A:HIS390 2.1 45.1 1.0 SG A:CYS404 2.3 47.2 1.0 SG A:CYS397 2.4 60.8 1.0 SG A:CYS396 2.4 53.6 1.0 CD2 A:HIS390 2.6 43.4 1.0 CE1 A:HIS390 3.3 45.1 1.0 CB A:CYS397 3.4 61.5 1.0 CB A:CYS404 3.5 63.1 1.0 CB A:CYS396 3.7 53.5 1.0 N A:CYS397 3.8 54.1 1.0 C A:CYS396 3.9 59.7 1.0 CG A:HIS390 3.9 46.9 1.0 N A:CYS404 4.1 79.9 1.0 O A:CYS396 4.1 64.8 1.0 CA A:CYS397 4.2 61.4 1.0 ND1 A:HIS390 4.2 43.3 1.0 CA A:CYS396 4.3 49.6 1.0 CA A:CYS404 4.4 70.7 1.0 O A:GLU402 4.5 57.1 1.0 NH1 A:ARG406 4.6 66.9 1.0 N A:GLY391 4.8 66.2 1.0 C A:CYS404 4.9 69.8 1.0 CA A:GLY391 4.9 64.9 1.0

Zinc binding site 2 out of 2 in the Human Cyclic Gmp-Amp Synthase (Cgas) in Complex with 2',2'-Cgamp


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Human Cyclic Gmp-Amp Synthase (Cgas) in Complex with 2',2'-Cgamp within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn601 b:66.4 occ:1.00 NE2 B:HIS390 2.1 39.5 1.0 SG B:CYS397 2.3 54.3 1.0 SG B:CYS404 2.3 48.0 1.0 SG B:CYS396 2.5 51.1 1.0 CD2 B:HIS390 2.7 37.9 1.0 CB B:CYS397 3.3 51.0 1.0 CE1 B:HIS390 3.3 48.4 1.0 CB B:CYS404 3.5 54.5 1.0 CB B:CYS396 3.7 54.1 1.0 N B:CYS397 3.8 49.4 1.0 C B:CYS396 3.9 54.8 1.0 CG B:HIS390 4.0 37.5 1.0 N B:CYS404 4.1 66.7 1.0 CA B:CYS397 4.1 50.6 1.0 O B:CYS396 4.2 65.7 1.0 ND1 B:HIS390 4.2 44.7 1.0 CA B:CYS404 4.3 57.6 1.0 CA B:CYS396 4.4 45.4 1.0 O B:GLU402 4.5 66.5 1.0 NH1 B:ARG406 4.8 37.7 1.0 C B:CYS404 4.8 56.7 1.0 N B:GLY391 5.0 41.7 1.0

J.Hall, E.C.Ralph, S.Shanker, H.Wang, L.J.Byrnes, R.Horst, J.Wong, A.Brault, D.Dumlao, J.F.Smith, L.A.Dakin, D.C.Schmitt, J.Trujillo, F.Vincent, M.Griffor, A.E.Aulabaugh. The Catalytic Mechanism of Cyclic Gmp-Amp Synthase (Cgas) and Implications For Innate Immunity and Inhibition. Protein Sci. V. 26 2367 2017.
ISSN: ESSN 1469-896X
PubMed: 28940468
DOI: 10.1002/PRO.3304