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Zinc in PDB 7c7e: Crystal Structure of C Terminal Domain of Escherichia Coli Dgor

Protein crystallography data

The structure of Crystal Structure of C Terminal Domain of Escherichia Coli Dgor, PDB code: 7c7e was solved by W.Lin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.01 / 2.05
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 85.037, 85.037, 111.688, 90, 90, 120
R / Rfree (%) 22.6 / 24.4

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of C Terminal Domain of Escherichia Coli Dgor (pdb code 7c7e). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of C Terminal Domain of Escherichia Coli Dgor, PDB code: 7c7e:

Zinc binding site 1 out of 1 in 7c7e

Go back to Zinc Binding Sites List in 7c7e
Zinc binding site 1 out of 1 in the Crystal Structure of C Terminal Domain of Escherichia Coli Dgor


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of C Terminal Domain of Escherichia Coli Dgor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:53.5
occ:1.00
OD1 A:ASP146 2.2 70.6 1.0
NE2 A:HIS195 2.2 54.2 1.0
NE2 A:HIS150 2.3 55.2 1.0
OD2 A:ASP146 2.5 69.2 1.0
CG A:ASP146 2.7 60.2 1.0
CE1 A:HIS195 2.9 44.6 1.0
CD2 A:HIS150 3.2 43.4 1.0
CE1 A:HIS150 3.3 48.7 1.0
CD2 A:HIS195 3.4 44.0 1.0
O2 A:SO4302 4.0 53.5 1.0
ND1 A:HIS195 4.2 45.0 1.0
CB A:ASP146 4.2 51.6 1.0
O4 A:SO4302 4.2 51.3 1.0
CG A:HIS150 4.4 44.8 1.0
ND1 A:HIS150 4.4 50.9 1.0
CG A:HIS195 4.4 50.7 1.0
O A:ASP146 4.7 48.9 1.0
S A:SO4302 4.8 52.5 1.0
CE A:MSE217 4.8 37.0 1.0
CA A:ASP146 4.9 54.6 1.0

Reference:

Z.Lin, Y.Sun, Y.Liu, S.Tong, Z.Shang, Y.Cai, W.Lin. Structural and Functional Analyses of the Transcription Repressor Dgor From Escherichia Coli Reveal A Divalent Metal-Containing D-Galactonate Binding Pocket. Front Microbiol V. 11 90330 2020.
ISSN: ESSN 1664-302X
PubMed: 33224125
DOI: 10.3389/FMICB.2020.590330
Page generated: Tue Oct 29 18:04:56 2024

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