Zinc in PDB 8imf: Human Cgas Catalytic Domain Bound with Baicalein

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

The structure of Human Cgas Catalytic Domain Bound with Baicalein, PDB code: 8imf was solved by W.F.Zhao, Y.C.Xu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.88 / 2.40
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	213.367, 45.981, 87.183, 90, 113.42, 90
R / Rfree (%)	22.8 / 27

The binding sites of Zinc atom in the Human Cgas Catalytic Domain Bound with Baicalein (pdb code 8imf). 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 Baicalein, PDB code: 8imf:
Jump to Zinc binding site number: 1; 2;

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


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 Baicalein within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn601 b:56.2 occ:1.00 NE2 A:HIS390 2.1 52.7 1.0 SG A:CYS396 2.4 55.5 1.0 SG A:CYS404 2.4 50.7 1.0 SG A:CYS397 2.5 49.2 1.0 CD2 A:HIS390 3.0 46.9 1.0 CE1 A:HIS390 3.2 52.8 1.0 CB A:CYS404 3.3 47.9 1.0 CB A:CYS397 3.4 55.1 1.0 CB A:CYS396 3.5 51.0 1.0 C A:CYS396 3.7 50.6 1.0 N A:CYS397 3.8 47.0 1.0 N A:CYS404 3.9 56.9 1.0 O A:CYS396 4.0 47.6 1.0 CA A:CYS404 4.1 57.1 1.0 CA A:CYS397 4.1 52.2 1.0 CG A:HIS390 4.2 55.4 1.0 CA A:CYS396 4.2 51.9 1.0 ND1 A:HIS390 4.2 53.3 1.0 NH1 A:ARG406 4.4 45.7 1.0 O A:GLU402 4.4 60.2 1.0 C A:CYS404 4.6 51.5 1.0 O A:CYS404 4.7 48.6 1.0

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


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 Baicalein within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn602 b:54.2 occ:1.00 NE2 B:HIS390 2.2 48.2 1.0 SG B:CYS397 2.3 49.8 1.0 SG B:CYS404 2.4 49.7 1.0 SG B:CYS396 2.5 49.4 1.0 CD2 B:HIS390 3.0 43.4 1.0 CE1 B:HIS390 3.3 47.1 1.0 CB B:CYS404 3.3 48.9 1.0 CB B:CYS397 3.3 54.3 1.0 CB B:CYS396 3.6 54.5 1.0 N B:CYS397 3.6 51.6 1.0 C B:CYS396 3.8 52.9 1.0 N B:CYS404 3.9 52.9 1.0 CA B:CYS397 4.0 57.8 1.0 CA B:CYS404 4.1 53.1 1.0 O B:CYS396 4.2 51.2 1.0 CA B:CYS396 4.2 51.6 1.0 CG B:HIS390 4.2 51.7 1.0 O B:GLU402 4.3 62.5 1.0 ND1 B:HIS390 4.3 50.5 1.0 NH1 B:ARG406 4.5 45.5 1.0 C B:CYS404 4.6 50.9 1.0 O B:CYS404 4.7 52.9 1.0 C B:LYS403 5.0 58.9 1.0

J.Li, M.Xiong, J.Liu, F.Zhang, M.Li, W.Zhao, Y.Xu. Discovery of Novel Cgas Inhibitors Based on Natural Flavonoids. Bioorg.Chem. V. 140 06802 2023.
ISSN: ISSN 0045-2068
PubMed: 37666112
DOI: 10.1016/J.BIOORG.2023.106802