Zinc in PDB 7buq: Mcgas Bound with 23-Cgamp

All present enzymatic activity of Mcgas Bound with 23-Cgamp:
2.7.7.86;

The structure of Mcgas Bound with 23-Cgamp, PDB code: 7buq 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)	37.72 / 3.09
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	47.645, 109.812, 75.637, 90.00, 94.13, 90.00
R / Rfree (%)	24.9 / 29.6

The binding sites of Zinc atom in the Mcgas Bound with 23-Cgamp (pdb code 7buq). 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 23-Cgamp, PDB code: 7buq:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Mcgas Bound with 23-Cgamp


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 23-Cgamp within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn601 b:46.1 occ:1.00 NE2 A:HIS378 2.1 32.7 1.0 SG A:CYS384 2.3 38.4 1.0 SG A:CYS392 2.3 37.9 1.0 SG A:CYS385 2.3 31.9 1.0 CD2 A:HIS378 2.8 33.1 1.0 CB A:CYS385 3.2 30.9 1.0 CE1 A:HIS378 3.3 32.9 1.0 CB A:CYS392 3.4 38.2 1.0 CB A:CYS384 3.5 38.6 1.0 N A:CYS385 3.6 32.2 1.0 C A:CYS384 3.6 38.4 1.0 CA A:CYS385 3.9 31.7 1.0 O A:CYS384 4.0 39.2 1.0 N A:CYS392 4.0 38.6 1.0 CG A:HIS378 4.1 33.4 1.0 CA A:CYS384 4.1 38.3 1.0 ND1 A:HIS378 4.2 33.2 1.0 CA A:CYS392 4.3 38.0 1.0 NH1 A:ARG394 4.3 34.8 1.0 O A:CYS392 4.7 38.7 1.0 C A:LYS391 4.7 40.3 1.0 C A:CYS392 4.8 38.4 1.0 O A:ALA390 4.9 26.4 1.0

Zinc binding site 2 out of 2 in the Mcgas Bound with 23-Cgamp


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 23-Cgamp within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn601 b:45.6 occ:1.00 NE2 B:HIS378 2.0 45.3 1.0 SG B:CYS385 2.2 44.9 1.0 SG B:CYS384 2.3 31.6 1.0 SG B:CYS392 2.3 56.8 1.0 CE1 B:HIS378 2.9 45.8 1.0 CD2 B:HIS378 3.0 45.7 1.0 CB B:CYS385 3.1 43.4 1.0 CB B:CYS392 3.4 56.7 1.0 N B:CYS385 3.5 44.4 1.0 CB B:CYS384 3.6 31.6 1.0 C B:CYS384 3.7 32.5 1.0 N B:CYS392 3.8 55.7 1.0 CA B:CYS385 3.9 43.6 1.0 ND1 B:HIS378 4.0 46.0 1.0 O B:CYS384 4.1 32.7 1.0 CG B:HIS378 4.1 46.2 1.0 CA B:CYS384 4.1 31.9 1.0 CA B:CYS392 4.2 56.1 1.0 NH1 B:ARG394 4.4 39.2 1.0 C B:LYS391 4.4 47.0 1.0 O B:ALA390 4.6 32.3 1.0 C B:CYS392 4.7 56.4 1.0 CA B:LYS391 4.8 46.9 1.0 O B:CYS392 4.8 57.0 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