Zinc in PDB 7uxw: Structure of Atp and Gtp Bind to Cyclic Gmp Amp Synthase (Cgas) Through Mg Coordination

All present enzymatic activity of Structure of Atp and Gtp Bind to Cyclic Gmp Amp Synthase (Cgas) Through Mg Coordination:
2.7.7.86;

The structure of Structure of Atp and Gtp Bind to Cyclic Gmp Amp Synthase (Cgas) Through Mg Coordination, PDB code: 7uxw was solved by S.Wu, S.B.Gabelli, J.Sohn, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.01 / 2.57
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	78.929, 98.66, 142.25, 90, 90, 90
R / Rfree (%)	19.7 / 24.8

The structure of Structure of Atp and Gtp Bind to Cyclic Gmp Amp Synthase (Cgas) Through Mg Coordination also contains other interesting chemical elements:

Magnesium

(Mg)

2 atoms

The binding sites of Zinc atom in the Structure of Atp and Gtp Bind to Cyclic Gmp Amp Synthase (Cgas) Through Mg Coordination (pdb code 7uxw). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structure of Atp and Gtp Bind to Cyclic Gmp Amp Synthase (Cgas) Through Mg Coordination, PDB code: 7uxw:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Structure of Atp and Gtp Bind to Cyclic Gmp Amp Synthase (Cgas) Through Mg Coordination


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Atp and Gtp Bind to Cyclic Gmp Amp Synthase (Cgas) Through Mg Coordination within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn604 b:40.4 occ:1.00 NE2 A:HIS378 2.0 40.3 1.0 SG A:CYS385 2.3 41.6 1.0 SG A:CYS384 2.3 40.3 1.0 SG A:CYS392 2.3 41.1 1.0 CD2 A:HIS378 2.9 39.4 1.0 CE1 A:HIS378 3.0 41.5 1.0 CB A:CYS392 3.4 38.3 1.0 CB A:CYS385 3.4 39.0 1.0 CB A:CYS384 3.5 36.6 1.0 N A:CYS392 3.7 40.5 1.0 N A:CYS385 3.7 36.5 1.0 C A:CYS384 3.8 36.9 1.0 CA A:CYS392 4.0 40.0 1.0 CG A:HIS378 4.1 39.8 1.0 ND1 A:HIS378 4.1 38.3 1.0 CA A:CYS385 4.1 36.1 1.0 CA A:CYS384 4.2 35.9 1.0 O A:CYS384 4.2 38.2 1.0 NH1 A:ARG394 4.3 46.6 1.0 C A:CYS392 4.6 39.1 1.0 O A:CYS392 4.7 43.9 1.0 C A:LYS391 4.8 43.1 1.0 O A:ALA390 4.8 43.9 1.0

Zinc binding site 2 out of 2 in the Structure of Atp and Gtp Bind to Cyclic Gmp Amp Synthase (Cgas) Through Mg Coordination


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of Atp and Gtp Bind to Cyclic Gmp Amp Synthase (Cgas) Through Mg Coordination within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn604 b:42.1 occ:1.00 NE2 C:HIS378 2.0 44.4 1.0 SG C:CYS385 2.3 43.1 1.0 SG C:CYS392 2.3 41.4 1.0 SG C:CYS384 2.3 41.9 1.0 CD2 C:HIS378 2.9 39.2 1.0 CE1 C:HIS378 3.0 41.5 1.0 CB C:CYS385 3.3 41.9 1.0 CB C:CYS392 3.4 41.5 1.0 CB C:CYS384 3.5 43.3 1.0 N C:CYS385 3.7 39.5 1.0 N C:CYS392 3.7 42.3 1.0 C C:CYS384 3.8 39.0 1.0 O C:HOH714 3.8 38.6 1.0 CG C:HIS378 4.1 37.7 1.0 CA C:CYS392 4.1 43.0 1.0 ND1 C:HIS378 4.1 35.6 1.0 CA C:CYS385 4.1 42.2 1.0 CA C:CYS384 4.1 39.8 1.0 O C:CYS384 4.2 34.9 1.0 NH1 C:ARG394 4.2 45.1 1.0 C C:CYS392 4.7 41.6 1.0 O C:CYS392 4.7 44.6 1.0 O C:ALA390 4.8 45.8 1.0 C C:LYS391 4.8 44.6 1.0

S.Wu, S.B.Gabelli, J.S.Sohn. Atp and Gtp Bind to Cyclic Gmp Amp Synthase (Cgas) Through Mg Coordination To Be Published.