Zinc in PDB 5vdu: Human Cyclic Gmp-Amp Synthase (Cgas) in Complex with Compound F2

All present enzymatic activity of Human Cyclic Gmp-Amp Synthase (Cgas) in Complex with Compound F2:
2.7.7.86;

The structure of Human Cyclic Gmp-Amp Synthase (Cgas) in Complex with Compound F2, PDB code: 5vdu 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)	52.27 / 2.73
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	216.415, 48.019, 86.466, 90.00, 104.94, 90.00
R / Rfree (%)	22.2 / 25.2

The binding sites of Zinc atom in the Human Cyclic Gmp-Amp Synthase (Cgas) in Complex with Compound F2 (pdb code 5vdu). 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 F2, PDB code: 5vdu:
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 F2


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 F2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn601 b:33.9 occ:1.00 NE2 A:HIS390 2.2 34.9 1.0 SG A:CYS404 2.3 40.1 1.0 SG A:CYS397 2.3 38.4 1.0 SG A:CYS396 2.4 39.5 1.0 CD2 A:HIS390 2.9 34.8 1.0 CE1 A:HIS390 3.3 33.5 1.0 CB A:CYS404 3.3 43.5 1.0 CB A:CYS397 3.4 40.2 1.0 CB A:CYS396 3.8 37.6 1.0 N A:CYS397 3.9 38.5 1.0 C A:CYS396 3.9 37.7 1.0 N A:CYS404 3.9 49.4 1.0 CA A:CYS404 4.1 48.0 1.0 CG A:HIS390 4.2 33.4 1.0 CA A:CYS397 4.2 40.9 1.0 O A:CYS396 4.2 37.4 1.0 NH1 A:ARG406 4.2 28.9 1.0 ND1 A:HIS390 4.3 32.2 1.0 CA A:CYS396 4.4 37.6 1.0 O A:GLU402 4.6 62.4 1.0 C A:CYS404 4.6 51.5 1.0 O A:CYS404 4.7 44.3 1.0

Zinc binding site 2 out of 2 in the Human Cyclic Gmp-Amp Synthase (Cgas) in Complex with Compound F2


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 F2 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn601 b:38.4 occ:1.00 NE2 B:HIS390 2.2 37.7 1.0 SG B:CYS397 2.3 38.6 1.0 SG B:CYS404 2.4 32.8 1.0 SG B:CYS396 2.4 32.6 1.0 CD2 B:HIS390 2.9 37.0 1.0 CE1 B:HIS390 3.3 36.8 1.0 CB B:CYS404 3.4 36.0 1.0 CB B:CYS397 3.4 39.8 1.0 CB B:CYS396 3.7 30.5 1.0 N B:CYS397 3.8 38.5 1.0 C B:CYS396 3.9 35.8 1.0 N B:CYS404 4.0 43.5 1.0 CG B:HIS390 4.1 35.8 1.0 CA B:CYS397 4.1 41.5 1.0 CA B:CYS404 4.2 38.9 1.0 O B:CYS396 4.2 36.3 1.0 O B:HOH722 4.2 22.4 1.0 ND1 B:HIS390 4.3 33.8 1.0 NH1 B:ARG406 4.3 29.4 1.0 CA B:CYS396 4.4 32.0 1.0 O B:GLU402 4.6 61.5 1.0 C B:CYS404 4.7 36.4 1.0 O B:CYS404 4.9 38.2 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