Zinc in PDB 5vdw: Human Cyclic Gmp-Amp Synthase (Cgas) in Complex with Compound F1

All present enzymatic activity of Human Cyclic Gmp-Amp Synthase (Cgas) in Complex with Compound F1:
2.7.7.86;

The structure of Human Cyclic Gmp-Amp Synthase (Cgas) in Complex with Compound F1, PDB code: 5vdw 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)	52.42 / 2.71
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	217.360, 47.998, 86.861, 90.00, 105.29, 90.00
R / Rfree (%)	22.2 / 25.7

The binding sites of Zinc atom in the Human Cyclic Gmp-Amp Synthase (Cgas) in Complex with Compound F1 (pdb code 5vdw). 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 F1, PDB code: 5vdw:
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 F1


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 F1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn601 b:46.0 occ:1.00 NE2 A:HIS390 2.2 38.1 1.0 SG A:CYS404 2.3 38.5 1.0 SG A:CYS397 2.3 38.6 1.0 SG A:CYS396 2.4 40.7 1.0 CD2 A:HIS390 2.8 38.6 1.0 CB A:CYS397 3.4 35.7 1.0 CB A:CYS404 3.4 35.5 1.0 CE1 A:HIS390 3.4 37.3 1.0 CB A:CYS396 3.8 36.1 1.0 N A:CYS397 3.9 29.9 1.0 C A:CYS396 3.9 33.3 1.0 N A:CYS404 4.1 34.0 1.0 NH1 A:ARG406 4.1 33.9 1.0 CG A:HIS390 4.1 32.6 1.0 CA A:CYS397 4.2 33.6 1.0 O A:CYS396 4.2 37.1 1.0 CA A:CYS404 4.3 36.5 1.0 ND1 A:HIS390 4.4 33.0 1.0 CA A:CYS396 4.4 31.4 1.0 C A:CYS404 4.8 36.5 1.0 O A:CYS404 4.9 44.6 1.0 O A:GLU402 4.9 58.9 1.0

Zinc binding site 2 out of 2 in the Human Cyclic Gmp-Amp Synthase (Cgas) in Complex with Compound F1


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 F1 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn601 b:47.0 occ:1.00 NE2 B:HIS390 2.1 26.0 1.0 SG B:CYS404 2.3 35.2 1.0 SG B:CYS397 2.3 33.8 1.0 SG B:CYS396 2.4 31.8 1.0 CD2 B:HIS390 2.7 28.0 1.0 CE1 B:HIS390 3.3 28.9 1.0 CB B:CYS397 3.4 31.5 1.0 CB B:CYS404 3.4 26.3 1.0 CB B:CYS396 3.8 35.0 1.0 N B:CYS397 3.9 30.8 1.0 C B:CYS396 3.9 31.1 1.0 CG B:HIS390 4.0 27.4 1.0 NH1 B:ARG406 4.1 24.7 1.0 N B:CYS404 4.1 42.1 1.0 CA B:CYS397 4.2 33.1 1.0 ND1 B:HIS390 4.2 28.0 1.0 O B:CYS396 4.3 30.7 1.0 CA B:CYS404 4.3 35.0 1.0 CA B:CYS396 4.4 31.4 1.0 C B:CYS404 4.8 37.0 1.0 O B:HOH710 4.9 27.3 1.0 O B:CYS404 4.9 35.1 1.0 O B:GLU402 4.9 56.5 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