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Zinc in PDB 7cv0: Crystal Structure of B. Halodurans Niar in Apo Form

Protein crystallography data

The structure of Crystal Structure of B. Halodurans Niar in Apo Form, PDB code: 7cv0 was solved by J.Y.Lee, D.W.Lee, Y.W.Park, M.Y.Lee, K.H.Jeong, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.93 / 2.00
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 42.365, 42.365, 176.203, 90.00, 90.00, 90.00
R / Rfree (%) 20.2 / 22.8

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of B. Halodurans Niar in Apo Form (pdb code 7cv0). 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 B. Halodurans Niar in Apo Form, PDB code: 7cv0:

Zinc binding site 1 out of 1 in 7cv0

Go back to Zinc Binding Sites List in 7cv0
Zinc binding site 1 out of 1 in the Crystal Structure of B. Halodurans Niar in Apo Form


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 B. Halodurans Niar in Apo Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn201

b:44.0
occ:1.00
OE1 A:GLU91 2.0 39.2 1.0
NE2 A:HIS152 2.0 20.7 1.0
NE2 A:HIS150 2.2 24.3 1.0
O A:HOH398 2.3 36.2 1.0
OE2 A:GLU91 2.5 25.3 1.0
CD A:GLU91 2.6 28.2 1.0
CD2 A:HIS150 2.9 20.3 1.0
CD2 A:HIS152 2.9 20.5 1.0
CE1 A:HIS152 3.1 23.3 1.0
CE1 A:HIS150 3.2 24.7 1.0
NE2 A:HIS83 3.8 31.6 1.0
CG A:HIS150 4.0 22.8 1.0
CG A:HIS152 4.1 22.0 1.0
CG A:GLU91 4.1 22.6 1.0
ND1 A:HIS152 4.1 22.9 1.0
ND1 A:HIS150 4.2 21.8 1.0
CD2 A:HIS83 4.2 28.3 1.0
CD2 A:LEU92 4.4 18.0 1.0
O A:HOH429 4.7 43.2 1.0
CB A:GLU91 4.8 23.1 1.0
CB A:CYS81 4.8 23.9 1.0
CG2 A:VAL105 4.9 18.7 1.0

Reference:

D.W.Lee, Y.W.Park, M.Y.Lee, K.H.Jeong, J.Y.Lee. Structural Analysis and Insight Into Effector Binding of the Niacin-Responsive Repressor Niar From Bacillus Halodurans. Sci Rep V. 10 21039 2020.
ISSN: ESSN 2045-2322
PubMed: 33273654
DOI: 10.1038/S41598-020-78148-X
Page generated: Tue Oct 29 18:27:26 2024

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