Zinc in PDB 7buj: Mcgas Bound with Pppgpg

All present enzymatic activity of Mcgas Bound with Pppgpg:
2.7.7.86;

The structure of Mcgas Bound with Pppgpg, PDB code: 7buj was solved by B.Wang, X.D.Su, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.71 / 2.13
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	47.798, 109.632, 75.501, 90.00, 93.52, 90.00
R / Rfree (%)	21.6 / 27.8

The structure of Mcgas Bound with Pppgpg also contains other interesting chemical elements:

Manganese

(Mn)

4 atoms

The binding sites of Zinc atom in the Mcgas Bound with Pppgpg (pdb code 7buj). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Mcgas Bound with Pppgpg, PDB code: 7buj:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Mcgas Bound with Pppgpg


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Mcgas Bound with Pppgpg within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn601 b:46.4 occ:1.00 NE2 A:HIS378 2.2 38.3 1.0 SG A:CYS384 2.2 47.9 1.0 SG A:CYS392 2.3 46.5 1.0 SG A:CYS385 2.4 46.6 1.0 CD2 A:HIS378 3.0 39.2 1.0 CB A:CYS385 3.4 45.9 1.0 CE1 A:HIS378 3.4 39.3 1.0 CB A:CYS392 3.4 46.0 1.0 CB A:CYS384 3.6 45.7 1.0 C A:CYS384 3.7 45.3 1.0 N A:CYS385 3.7 49.0 1.0 N A:CYS392 3.8 47.7 1.0 O A:CYS384 4.0 46.4 1.0 O A:HOH761 4.1 49.4 1.0 CA A:CYS385 4.1 48.4 1.0 CA A:CYS392 4.1 50.2 1.0 CA A:CYS384 4.1 49.0 1.0 CG A:HIS378 4.2 40.1 1.0 ND1 A:HIS378 4.4 39.3 1.0 C A:CYS392 4.7 48.2 1.0 O A:ALA390 4.7 58.9 1.0 C A:LYS391 4.8 58.3 1.0 O A:CYS392 4.8 46.6 1.0

Zinc binding site 2 out of 2 in the Mcgas Bound with Pppgpg


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Mcgas Bound with Pppgpg within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn601 b:45.6 occ:1.00 NE2 B:HIS378 2.0 41.3 1.0 SG B:CYS392 2.2 46.2 1.0 SG B:CYS385 2.3 43.1 1.0 SG B:CYS384 2.4 42.1 1.0 CD2 B:HIS378 2.9 39.1 1.0 CE1 B:HIS378 3.1 42.5 1.0 CB B:CYS385 3.4 41.5 1.0 CB B:CYS392 3.4 46.8 1.0 CB B:CYS384 3.6 41.5 1.0 N B:CYS385 3.7 44.5 1.0 C B:CYS384 3.7 40.9 1.0 O B:HOH748 3.9 50.4 1.0 N B:CYS392 3.9 46.9 1.0 O B:CYS384 3.9 41.7 1.0 CA B:CYS385 4.1 43.2 1.0 CG B:HIS378 4.1 41.9 1.0 CA B:CYS384 4.2 42.5 1.0 CA B:CYS392 4.2 46.5 1.0 ND1 B:HIS378 4.2 41.7 1.0 NH1 B:ARG394 4.2 47.1 1.0 O B:HOH741 4.4 55.6 1.0 O B:CYS392 4.6 47.2 1.0 C B:CYS392 4.6 47.1 1.0 O B:ALA390 4.8 50.9 1.0 C B:LYS391 4.9 54.5 1.0

Z.Zhao, Z.Ma, B.Wang, Y.Guan, X.D.Su, Z.Jiang. MN2+Directly Activates Cgas and Structural Analysis Suggests MN2+Induces A Noncanonical Catalytic Synthesis of 2'3'-Cgamp. Cell Rep V. 32 08053 2020.
ISSN: ESSN 2211-1247
PubMed: 32814054
DOI: 10.1016/J.CELREP.2020.108053