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Nickel in PDB 3idq: Crystal Structure of S. Cerevisiae GET3 at 3.7 Angstrom Resolution

Enzymatic activity of Crystal Structure of S. Cerevisiae GET3 at 3.7 Angstrom Resolution

All present enzymatic activity of Crystal Structure of S. Cerevisiae GET3 at 3.7 Angstrom Resolution:
3.6.3.16;

Protein crystallography data

The structure of Crystal Structure of S. Cerevisiae GET3 at 3.7 Angstrom Resolution, PDB code: 3idq was solved by C.J.M.Suloway, J.W.Chartron, M.Zaslaver, W.M.Clemons Jr., with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.05 / 3.70
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 115.320, 115.320, 281.111, 90.00, 90.00, 120.00
R / Rfree (%) 28.3 / 33.5

Nickel Binding Sites:

The binding sites of Nickel atom in the Crystal Structure of S. Cerevisiae GET3 at 3.7 Angstrom Resolution (pdb code 3idq). This binding sites where shown within 5.0 Angstroms radius around Nickel atom.
In total only one binding site of Nickel was determined in the Crystal Structure of S. Cerevisiae GET3 at 3.7 Angstrom Resolution, PDB code: 3idq:

Nickel binding site 1 out of 1 in 3idq

Go back to Nickel Binding Sites List in 3idq
Nickel binding site 1 out of 1 in the Crystal Structure of S. Cerevisiae GET3 at 3.7 Angstrom Resolution


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 1 of Crystal Structure of S. Cerevisiae GET3 at 3.7 Angstrom Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ni370

b:59.0
occ:0.33
CE1 A:HIS367 2.2 0.6 1.0
NE2 A:HIS369 2.2 0.4 1.0
NE2 A:HIS367 2.5 0.6 1.0
CD2 A:HIS369 2.8 0.4 1.0
ND1 A:HIS367 3.4 0.6 1.0
CE1 A:HIS369 3.4 0.4 1.0
CD2 A:HIS367 3.8 0.6 1.0
CG A:HIS369 4.1 0.4 1.0
CG A:HIS367 4.2 0.6 1.0
ND1 A:HIS369 4.3 0.4 1.0

Reference:

C.J.Suloway, J.W.Chartron, M.Zaslaver, W.M.Clemons. Model For Eukaryotic Tail-Anchored Protein Binding Based on the Structure of GET3 Proc.Natl.Acad.Sci.Usa V. 106 14849 2009.
ISSN: ISSN 0027-8424
PubMed: 19706470
DOI: 10.1073/PNAS.0907522106
Page generated: Fri Sep 25 08:24:57 2020
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