Zinc in PDB 6o47: Human Cgas Core Domain (K427E/K428E) Bound with Ru-521

All present enzymatic activity of Human Cgas Core Domain (K427E/K428E) Bound with Ru-521:
2.7.7.86;

The structure of Human Cgas Core Domain (K427E/K428E) Bound with Ru-521, PDB code: 6o47 was solved by W.Xie, L.Lama, C.Adura, J.F.Glickman, T.Tuschl, D.J.Patel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.27 / 2.20
Space group	P 64
Cell size a, b, c (Å), α, β, γ (°)	116.157, 116.157, 59.951, 90.00, 90.00, 120.00
R / Rfree (%)	18.2 / 22.1

The structure of Human Cgas Core Domain (K427E/K428E) Bound with Ru-521 also contains other interesting chemical elements:

Chlorine

(Cl)

4 atoms

The binding sites of Zinc atom in the Human Cgas Core Domain (K427E/K428E) Bound with Ru-521 (pdb code 6o47). 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 Cgas Core Domain (K427E/K428E) Bound with Ru-521, PDB code: 6o47:

Zinc binding site 1 out of 1 in the Human Cgas Core Domain (K427E/K428E) Bound with Ru-521


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Cgas Core Domain (K427E/K428E) Bound with Ru-521 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn603 b:19.2 occ:1.00 NE2 A:HIS390 2.2 20.7 1.0 SG A:CYS396 2.3 17.8 1.0 SG A:CYS397 2.3 20.4 1.0 SG A:CYS404 2.4 18.2 1.0 CD2 A:HIS390 2.9 13.9 1.0 CE1 A:HIS390 3.3 18.7 1.0 CB A:CYS397 3.4 20.8 1.0 CB A:CYS404 3.4 16.8 1.0 CB A:CYS396 3.5 16.2 1.0 N A:CYS397 3.6 20.6 1.0 O A:HOH828 3.7 18.4 1.0 C A:CYS396 3.7 19.9 1.0 N A:CYS404 3.8 22.1 1.0 CA A:CYS397 4.1 23.1 1.0 CA A:CYS404 4.1 20.2 1.0 CA A:CYS396 4.1 19.0 1.0 O A:CYS396 4.2 17.8 1.0 CG A:HIS390 4.2 17.3 1.0 ND1 A:HIS390 4.3 17.7 1.0 O A:GLU402 4.3 29.8 1.0 NH1 A:ARG406 4.4 14.2 1.0 O A:CYS404 4.5 19.6 1.0 C A:CYS404 4.6 20.7 1.0 O A:HOH868 4.7 27.5 1.0 O A:HOH813 4.7 25.4 1.0 O A:HOH830 4.8 17.6 1.0 C A:LYS403 4.9 29.1 1.0

W.Xie, L.Lama, C.Adura, D.Tomita, J.F.Glickman, T.Tuschl, D.J.Patel. Human Cgas Catalytic Domain Has An Additional Dna-Binding Interface That Enhances Enzymatic Activity and Liquid-Phase Condensation. Proc.Natl.Acad.Sci.Usa V. 116 11946 2019.
ISSN: ESSN 1091-6490
PubMed: 31142647
DOI: 10.1073/PNAS.1905013116