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

Enzymatic activity of Mcgas Bound with 23-Cgamp

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

Protein crystallography data

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

Zinc Binding Sites:

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 7buq

Go back to Zinc Binding Sites List in 7buq
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 7buq

Go back to Zinc Binding Sites List in 7buq
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

Reference:

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
Page generated: Wed Dec 16 13:37:03 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy