Zinc in PDB 7bum: Mcgas Bound with Pgpa

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

The structure of Mcgas Bound with Pgpa, PDB code: 7bum 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)	30.82 / 3.05
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	48.337, 109.592, 75.870, 90.00, 93.93, 90.00
R / Rfree (%)	21.7 / 28

The binding sites of Zinc atom in the Mcgas Bound with Pgpa (pdb code 7bum). 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 Pgpa, PDB code: 7bum:
Jump to Zinc binding site number: 1; 2;

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


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 Pgpa within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn601 b:47.9 occ:1.00 SG A:CYS392 2.2 60.9 1.0 SG A:CYS385 2.2 34.5 1.0 NE2 A:HIS378 2.3 53.9 1.0 SG A:CYS384 2.5 54.9 1.0 CD2 A:HIS378 2.9 52.9 1.0 CB A:CYS392 3.4 61.5 1.0 CE1 A:HIS378 3.4 53.8 1.0 CB A:CYS385 3.5 38.7 1.0 N A:CYS385 3.7 42.3 1.0 CB A:CYS384 3.8 52.5 1.0 N A:CYS392 3.8 61.2 1.0 C A:CYS384 4.1 56.1 1.0 CG A:HIS378 4.1 52.3 1.0 CA A:CYS385 4.1 39.7 1.0 CA A:CYS392 4.1 59.5 1.0 NH1 A:ARG394 4.3 56.9 1.0 ND1 A:HIS378 4.3 53.0 1.0 CA A:CYS384 4.4 54.0 1.0 C A:CYS392 4.7 59.8 1.0 O A:ALA390 4.7 43.5 1.0 O A:CYS384 4.8 56.0 1.0 C A:LYS391 4.8 59.0 1.0 O A:CYS392 4.9 62.2 1.0 N A:GLY379 4.9 45.2 1.0 CA A:GLY379 5.0 45.6 1.0

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


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 Pgpa within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn601 b:49.6 occ:1.00 NE2 B:HIS378 2.0 50.4 1.0 SG B:CYS385 2.4 43.5 1.0 SG B:CYS384 2.4 47.0 1.0 SG B:CYS392 2.5 60.3 1.0 CD2 B:HIS378 2.6 48.7 1.0 CE1 B:HIS378 3.2 50.3 1.0 CB B:CYS392 3.3 58.3 1.0 CB B:CYS384 3.5 41.5 1.0 CB B:CYS385 3.5 45.6 1.0 CG B:HIS378 3.9 49.0 1.0 C B:CYS384 3.9 44.5 1.0 N B:CYS385 4.0 46.3 1.0 N B:CYS392 4.0 57.2 1.0 NH1 B:ARG394 4.0 47.8 1.0 O B:CYS384 4.1 46.4 1.0 ND1 B:HIS378 4.1 49.6 1.0 CA B:CYS392 4.2 56.9 1.0 CA B:CYS384 4.3 43.0 1.0 CA B:CYS385 4.4 47.2 1.0 C B:CYS392 4.8 57.9 1.0 O B:ALA390 4.8 50.9 1.0 C B:LYS391 4.9 57.2 1.0 O B:CYS392 5.0 58.6 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