Zinc in PDB 8imf: Human Cgas Catalytic Domain Bound with Baicalein

Enzymatic activity of Human Cgas Catalytic Domain Bound with Baicalein

All present enzymatic activity of Human Cgas Catalytic Domain Bound with Baicalein:
2.7.7.86;

Protein crystallography data

The structure of Human Cgas Catalytic Domain Bound with Baicalein, PDB code: 8imf was solved by W.F.Zhao, Y.C.Xu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.88 / 2.40
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 213.367, 45.981, 87.183, 90, 113.42, 90
R / Rfree (%) 22.8 / 27

Zinc Binding Sites:

The binding sites of Zinc atom in the Human Cgas Catalytic Domain Bound with Baicalein (pdb code 8imf). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Human Cgas Catalytic Domain Bound with Baicalein, PDB code: 8imf:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 8imf

Go back to Zinc Binding Sites List in 8imf
Zinc binding site 1 out of 2 in the Human Cgas Catalytic Domain Bound with Baicalein


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Cgas Catalytic Domain Bound with Baicalein within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn601

b:56.2
occ:1.00
NE2 A:HIS390 2.1 52.7 1.0
SG A:CYS396 2.4 55.5 1.0
SG A:CYS404 2.4 50.7 1.0
SG A:CYS397 2.5 49.2 1.0
CD2 A:HIS390 3.0 46.9 1.0
CE1 A:HIS390 3.2 52.8 1.0
CB A:CYS404 3.3 47.9 1.0
CB A:CYS397 3.4 55.1 1.0
CB A:CYS396 3.5 51.0 1.0
C A:CYS396 3.7 50.6 1.0
N A:CYS397 3.8 47.0 1.0
N A:CYS404 3.9 56.9 1.0
O A:CYS396 4.0 47.6 1.0
CA A:CYS404 4.1 57.1 1.0
CA A:CYS397 4.1 52.2 1.0
CG A:HIS390 4.2 55.4 1.0
CA A:CYS396 4.2 51.9 1.0
ND1 A:HIS390 4.2 53.3 1.0
NH1 A:ARG406 4.4 45.7 1.0
O A:GLU402 4.4 60.2 1.0
C A:CYS404 4.6 51.5 1.0
O A:CYS404 4.7 48.6 1.0

Zinc binding site 2 out of 2 in 8imf

Go back to Zinc Binding Sites List in 8imf
Zinc binding site 2 out of 2 in the Human Cgas Catalytic Domain Bound with Baicalein


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Human Cgas Catalytic Domain Bound with Baicalein within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn602

b:54.2
occ:1.00
NE2 B:HIS390 2.2 48.2 1.0
SG B:CYS397 2.3 49.8 1.0
SG B:CYS404 2.4 49.7 1.0
SG B:CYS396 2.5 49.4 1.0
CD2 B:HIS390 3.0 43.4 1.0
CE1 B:HIS390 3.3 47.1 1.0
CB B:CYS404 3.3 48.9 1.0
CB B:CYS397 3.3 54.3 1.0
CB B:CYS396 3.6 54.5 1.0
N B:CYS397 3.6 51.6 1.0
C B:CYS396 3.8 52.9 1.0
N B:CYS404 3.9 52.9 1.0
CA B:CYS397 4.0 57.8 1.0
CA B:CYS404 4.1 53.1 1.0
O B:CYS396 4.2 51.2 1.0
CA B:CYS396 4.2 51.6 1.0
CG B:HIS390 4.2 51.7 1.0
O B:GLU402 4.3 62.5 1.0
ND1 B:HIS390 4.3 50.5 1.0
NH1 B:ARG406 4.5 45.5 1.0
C B:CYS404 4.6 50.9 1.0
O B:CYS404 4.7 52.9 1.0
C B:LYS403 5.0 58.9 1.0

Reference:

J.Li, M.Xiong, J.Liu, F.Zhang, M.Li, W.Zhao, Y.Xu. Discovery of Novel Cgas Inhibitors Based on Natural Flavonoids. Bioorg.Chem. V. 140 06802 2023.
ISSN: ISSN 0045-2068
PubMed: 37666112
DOI: 10.1016/J.BIOORG.2023.106802
Page generated: Thu Oct 31 07:54:06 2024

Last articles

Zn in 9J0N
Zn in 9J0O
Zn in 9J0P
Zn in 9FJX
Zn in 9EKB
Zn in 9C0F
Zn in 9CAH
Zn in 9CH0
Zn in 9CH3
Zn in 9CH1
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy