Zinc in PDB 5vdv: Human Cyclic Gmp-Amp Synthase (Cgas) in Complex with Compound F3

All present enzymatic activity of Human Cyclic Gmp-Amp Synthase (Cgas) in Complex with Compound F3:
2.7.7.86;

The structure of Human Cyclic Gmp-Amp Synthase (Cgas) in Complex with Compound F3, PDB code: 5vdv 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)	55.27 / 3.00
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	217.448, 46.953, 89.733, 90.00, 111.43, 90.00
R / Rfree (%)	20.5 / 25.7

The binding sites of Zinc atom in the Human Cyclic Gmp-Amp Synthase (Cgas) in Complex with Compound F3 (pdb code 5vdv). 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 Compound F3, PDB code: 5vdv:
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 Compound F3


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 Compound F3 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn601 b:81.4 occ:1.00 NE2 A:HIS390 2.1 70.7 1.0 SG A:CYS397 2.2 66.8 1.0 SG A:CYS404 2.2 58.8 1.0 SG A:CYS396 2.4 67.8 1.0 CD2 A:HIS390 2.5 68.7 1.0 CE1 A:HIS390 3.4 69.3 1.0 CB A:CYS404 3.4 60.8 1.0 CB A:CYS397 3.5 67.4 1.0 O A:HOH731 3.6 52.0 1.0 CB A:CYS396 3.8 65.8 1.0 CG A:HIS390 3.8 59.3 1.0 N A:CYS397 4.0 66.4 1.0 N A:CYS404 4.0 66.1 1.0 C A:CYS396 4.0 63.6 1.0 ND1 A:HIS390 4.2 63.5 1.0 CA A:CYS404 4.2 65.7 1.0 NH1 A:ARG406 4.3 60.8 1.0 CA A:CYS397 4.3 70.0 1.0 O A:CYS396 4.3 70.5 1.0 CA A:CYS396 4.4 62.1 1.0 O A:GLU402 4.5 88.4 1.0 C A:CYS404 4.7 69.3 1.0 N A:GLY391 4.8 62.9 1.0 O A:CYS404 4.9 79.0 1.0 CA A:GLY391 4.9 61.7 1.0

Zinc binding site 2 out of 2 in the Human Cyclic Gmp-Amp Synthase (Cgas) in Complex with Compound F3


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 Compound F3 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn601 b:71.6 occ:1.00 NE2 B:HIS390 2.1 64.8 1.0 SG B:CYS397 2.2 67.7 1.0 SG B:CYS396 2.3 70.2 1.0 SG B:CYS404 2.3 69.1 1.0 CD2 B:HIS390 2.6 58.8 1.0 CE1 B:HIS390 3.3 68.3 1.0 CB B:CYS404 3.4 67.4 1.0 CB B:CYS397 3.5 67.7 1.0 CB B:CYS396 3.7 64.0 1.0 CG B:HIS390 3.9 53.2 1.0 N B:CYS397 3.9 69.2 1.0 N B:CYS404 4.0 64.6 1.0 C B:CYS396 4.0 67.2 1.0 NH1 B:ARG406 4.2 76.0 1.0 CA B:CYS404 4.2 65.7 1.0 ND1 B:HIS390 4.2 60.4 1.0 O B:CYS396 4.3 70.4 1.0 CA B:CYS397 4.3 71.0 1.0 CA B:CYS396 4.4 64.5 1.0 O B:GLU402 4.5 0.8 1.0 C B:CYS404 4.7 62.4 1.0 N B:GLY391 4.9 56.8 1.0 O B:CYS404 4.9 74.5 1.0 CA B:GLY391 4.9 59.0 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