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Nickel in PDB 1gub: Hinge-Bending Motion of D-Allose Binding Protein From Escherichia Coli: Three Open Conformations

Protein crystallography data

The structure of Hinge-Bending Motion of D-Allose Binding Protein From Escherichia Coli: Three Open Conformations, PDB code: 1gub was solved by U.Magnusson, B.N.Chaudhuri, J.Ko, C.Park, T.A.Jones, S.L.Mowbray, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.75 / 3.10
Space group P 4 3 2
Cell size a, b, c (Å), α, β, γ (°) 133.100, 133.100, 133.100, 90.00, 90.00, 90.00
R / Rfree (%) 28 / 33.9

Nickel Binding Sites:

The binding sites of Nickel atom in the Hinge-Bending Motion of D-Allose Binding Protein From Escherichia Coli: Three Open Conformations (pdb code 1gub). 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 Hinge-Bending Motion of D-Allose Binding Protein From Escherichia Coli: Three Open Conformations, PDB code: 1gub:

Nickel binding site 1 out of 1 in 1gub

Go back to Nickel Binding Sites List in 1gub
Nickel binding site 1 out of 1 in the Hinge-Bending Motion of D-Allose Binding Protein From Escherichia Coli: Three Open Conformations


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 1 of Hinge-Bending Motion of D-Allose Binding Protein From Escherichia Coli: Three Open Conformations within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ni1289

b:22.1
occ:0.33
CB A:ALA1 1.2 0.0 1.0
O A:HOH2001 2.5 2.0 0.3
CA A:ALA1 2.8 0.7 1.0
N A:ALA1 2.9 0.4 1.0
C A:ALA1 3.4 0.5 1.0
O A:ALA1 3.8 0.7 1.0
O A:HOH2002 4.3 7.7 1.0
N A:ALA2 4.7 47.0 1.0

Reference:

B.N.Chaudhuri, J.Ko, C.Park, T.A.Jones, S.L.Mowbray. Structure of D-Allose Binding Protein From Escherichia Coli Bound to D-Allose at 1.8 A Resolution J.Mol.Biol. V. 286 1519 1999.
ISSN: ISSN 0022-2836
PubMed: 10064713
DOI: 10.1006/JMBI.1999.2571
Page generated: Wed Dec 16 01:12:01 2020

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