Zinc in PDB 6lre: Human Cgas Catalytic Domain Bound with Compound 3

All present enzymatic activity of Human Cgas Catalytic Domain Bound with Compound 3:
2.7.7.86;

The structure of Human Cgas Catalytic Domain Bound with Compound 3, PDB code: 6lre 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)	38.41 / 2.65
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	213.607, 47.536, 87.758, 90.00, 113.72, 90.00
R / Rfree (%)	21.5 / 26.8

The binding sites of Zinc atom in the Human Cgas Catalytic Domain Bound with Compound 3 (pdb code 6lre). 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 3, PDB code: 6lre:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Human Cgas Catalytic Domain Bound with Compound 3


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 3 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn601 b:32.8 occ:1.00 SG A:CYS397 2.3 30.5 1.0 SG A:CYS404 2.3 20.9 1.0 NE2 A:HIS390 2.3 17.8 1.0 SG A:CYS396 2.4 20.9 1.0 CD2 A:HIS390 3.0 16.4 1.0 CB A:CYS397 3.2 31.2 1.0 CB A:CYS404 3.3 26.5 1.0 CE1 A:HIS390 3.4 21.1 1.0 O A:HOH713 3.5 16.9 1.0 CB A:CYS396 3.6 31.0 1.0 N A:CYS397 3.7 14.6 1.0 C A:CYS396 3.7 27.1 1.0 N A:CYS404 3.8 24.7 1.0 CA A:CYS397 4.0 26.7 1.0 O A:CYS396 4.0 28.0 1.0 CA A:CYS404 4.1 25.6 1.0 CA A:CYS396 4.2 27.3 1.0 CG A:HIS390 4.3 21.7 1.0 ND1 A:HIS390 4.4 20.8 1.0 O A:CYS404 4.5 33.0 1.0 C A:CYS404 4.5 27.7 1.0 NH1 A:ARG406 4.5 28.8 1.0 O A:GLU402 4.5 37.4 1.0 C A:LYS403 5.0 30.9 1.0

Zinc binding site 2 out of 2 in the Human Cgas Catalytic Domain Bound with Compound 3


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 3 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn601 b:30.4 occ:1.00 NE2 B:HIS390 2.3 23.6 1.0 SG B:CYS397 2.3 28.7 1.0 SG B:CYS404 2.3 14.4 1.0 SG B:CYS396 2.4 34.9 1.0 CD2 B:HIS390 3.0 24.6 1.0 CB B:CYS397 3.2 30.9 1.0 CB B:CYS404 3.4 17.2 1.0 CE1 B:HIS390 3.4 27.4 1.0 O B:HOH719 3.6 16.6 1.0 CB B:CYS396 3.7 36.4 1.0 N B:CYS397 3.7 22.1 1.0 C B:CYS396 3.8 25.6 1.0 N B:CYS404 3.8 31.5 1.0 CA B:CYS397 4.0 30.3 1.0 CA B:CYS404 4.1 28.3 1.0 O B:CYS396 4.1 26.2 1.0 CG B:HIS390 4.3 28.0 1.0 CA B:CYS396 4.3 25.0 1.0 ND1 B:HIS390 4.4 27.9 1.0 NH1 B:ARG406 4.5 29.5 1.0 C B:CYS404 4.5 35.2 1.0 O B:CYS404 4.5 40.7 1.0 O B:GLU402 4.6 50.3 1.0 C B:LYS403 5.0 39.2 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