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Nickel in PDB 2wja: Crystal Structure of the Tyrosine Phosphatase Wzb From Escherichia Coli K30 in Complex with Phosphate.

Protein crystallography data

The structure of Crystal Structure of the Tyrosine Phosphatase Wzb From Escherichia Coli K30 in Complex with Phosphate., PDB code: 2wja was solved by H.Huang, G.Hagelueken, C.Whitfield, J.H.Naismith, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.500 / 2.50
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 90.030, 90.030, 83.540, 90.00, 90.00, 120.00
R / Rfree (%) 21.98 / 26.84

Nickel Binding Sites:

The binding sites of Nickel atom in the Crystal Structure of the Tyrosine Phosphatase Wzb From Escherichia Coli K30 in Complex with Phosphate. (pdb code 2wja). 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 the Tyrosine Phosphatase Wzb From Escherichia Coli K30 in Complex with Phosphate., PDB code: 2wja:

Nickel binding site 1 out of 1 in 2wja

Go back to Nickel Binding Sites List in 2wja
Nickel binding site 1 out of 1 in the Crystal Structure of the Tyrosine Phosphatase Wzb From Escherichia Coli K30 in Complex with Phosphate.


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 the Tyrosine Phosphatase Wzb From Escherichia Coli K30 in Complex with Phosphate. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ni1149

b:53.1
occ:0.73
NE2 A:HIS47 2.5 65.4 1.0
CD2 A:HIS47 3.2 68.7 1.0
CE1 A:HIS47 3.5 71.8 1.0
CG A:HIS47 4.4 64.8 1.0
ND1 A:HIS47 4.6 77.2 1.0
O A:VAL45 4.6 67.5 1.0

Reference:

G.Hagelueken, H.Huang, I.L.Mainprize, C.Whitfield, J.H.Naismith. Crystal Structures of Wzb of Escherichia Coli and Cpsb of Streptococcus Pneumoniae, Representatives of Two Families of Tyrosine Phosphatases That Regulate Capsule Assembly. J.Mol.Biol. V. 392 678 2009.
ISSN: ISSN 0022-2836
PubMed: 19616007
DOI: 10.1016/J.JMB.2009.07.026
Page generated: Fri Sep 25 08:16:14 2020
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