Zinc in PDB 6lrk: Human Cgas Catalytic Domain Bound with Compound 40

All present enzymatic activity of Human Cgas Catalytic Domain Bound with Compound 40:
2.7.7.86;

The structure of Human Cgas Catalytic Domain Bound with Compound 40, PDB code: 6lrk was solved by W.F.Zhao, M.Y.Xiong, X.J.Yuan, H.B.Sun, Y.C.Xu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	32.32 / 2.25
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	216.188, 45.916, 84.960, 90.00, 113.29, 90.00
R / Rfree (%)	18.6 / 23.8

The binding sites of Zinc atom in the Human Cgas Catalytic Domain Bound with Compound 40 (pdb code 6lrk). 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 Cgas Catalytic Domain Bound with Compound 40, PDB code: 6lrk:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Human Cgas Catalytic Domain Bound with Compound 40


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Cgas Catalytic Domain Bound with Compound 40 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn602 b:20.4 occ:1.00 NE2 A:HIS390 2.2 22.7 1.0 SG A:CYS397 2.3 16.8 1.0 SG A:CYS396 2.3 19.3 1.0 SG A:CYS404 2.4 12.0 1.0 CD2 A:HIS390 3.0 14.9 1.0 CB A:CYS397 3.2 11.9 1.0 CE1 A:HIS390 3.3 20.0 1.0 CB A:CYS404 3.3 11.8 1.0 O A:HOH762 3.6 22.4 1.0 CB A:CYS396 3.7 11.2 1.0 N A:CYS397 3.8 20.9 1.0 N A:CYS404 3.9 16.2 1.0 C A:CYS396 3.9 14.7 1.0 CA A:CYS397 4.0 17.5 1.0 CA A:CYS404 4.1 23.8 1.0 O A:CYS396 4.2 21.2 1.0 CG A:HIS390 4.2 20.4 1.0 CA A:CYS396 4.3 11.8 1.0 ND1 A:HIS390 4.3 19.7 1.0 O A:GLU402 4.4 24.0 1.0 NH1 A:ARG406 4.4 11.8 1.0 O A:HOH768 4.5 33.1 1.0 C A:CYS404 4.6 16.2 1.0 O A:CYS404 4.6 18.1 1.0 C A:LYS403 4.9 20.6 1.0 O A:HOH746 5.0 27.8 1.0

Zinc binding site 2 out of 2 in the Human Cgas Catalytic Domain Bound with Compound 40


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Human Cgas Catalytic Domain Bound with Compound 40 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn602 b:24.8 occ:1.00 NE2 B:HIS390 2.2 21.8 1.0 SG B:CYS397 2.3 18.3 1.0 SG B:CYS396 2.4 18.4 1.0 SG B:CYS404 2.4 12.6 1.0 CD2 B:HIS390 3.0 18.3 1.0 CE1 B:HIS390 3.3 23.2 1.0 CB B:CYS397 3.3 15.4 1.0 CB B:CYS404 3.4 10.7 1.0 O B:HOH777 3.5 30.9 1.0 CB B:CYS396 3.7 19.4 1.0 N B:CYS397 3.7 15.3 1.0 C B:CYS396 3.8 12.2 1.0 N B:CYS404 3.9 15.9 1.0 CA B:CYS397 4.0 21.9 1.0 CA B:CYS404 4.1 18.8 1.0 O B:CYS396 4.2 14.8 1.0 CG B:HIS390 4.2 19.5 1.0 CA B:CYS396 4.3 14.1 1.0 ND1 B:HIS390 4.3 19.3 1.0 NH1 B:ARG406 4.3 10.5 1.0 O B:GLU402 4.4 19.7 1.0 O B:HOH782 4.5 35.0 1.0 C B:CYS404 4.5 18.0 1.0 O B:CYS404 4.6 17.9 1.0

W.F.Zhao, M.Y.Xiong, X.J.Yuan, M.J.Li, H.B.Sun, Y.C.Xu. In Silico Screening-Based Discovery of Novel Inhibitors of Human Cyclic Gmp-Amp Synthase: A Cross-Validation Study of Molecular Docking and Experimental Testing. J.Chem.Inf.Model. 2020.
ISSN: ESSN 1549-960X
PubMed: 32459092
DOI: 10.1021/ACS.JCIM.0C00171