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Chlorine in PDB 3ses: Cu-Mediated Dimer of Maltose-Binding Protein A216H/K220H By Synthetic Symmetrization

Protein crystallography data

The structure of Cu-Mediated Dimer of Maltose-Binding Protein A216H/K220H By Synthetic Symmetrization, PDB code: 3ses was solved by M.Zhao, A.B.Soriaga, A.Laganowsky, M.R.Sawaya, D.Cascio, T.O.Yeates, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 64.98 / 1.90
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 72.850, 61.250, 89.450, 90.00, 109.71, 90.00
R / Rfree (%) 17.2 / 20.5

Other elements in 3ses:

The structure of Cu-Mediated Dimer of Maltose-Binding Protein A216H/K220H By Synthetic Symmetrization also contains other interesting chemical elements:

Copper (Cu) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Cu-Mediated Dimer of Maltose-Binding Protein A216H/K220H By Synthetic Symmetrization (pdb code 3ses). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Cu-Mediated Dimer of Maltose-Binding Protein A216H/K220H By Synthetic Symmetrization, PDB code: 3ses:

Chlorine binding site 1 out of 1 in 3ses

Go back to Chlorine Binding Sites List in 3ses
Chlorine binding site 1 out of 1 in the Cu-Mediated Dimer of Maltose-Binding Protein A216H/K220H By Synthetic Symmetrization


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Cu-Mediated Dimer of Maltose-Binding Protein A216H/K220H By Synthetic Symmetrization within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl375

b:41.3
occ:1.00
O A:HOH540 2.9 34.2 1.0
O A:HOH572 3.2 36.2 1.0
N A:TYR177 3.2 26.2 1.0
CD2 A:TYR177 3.7 20.4 1.0
CA A:LYS176 3.8 31.8 1.0
CG2 A:ILE334 3.8 18.9 1.0
CB A:LYS176 3.8 38.3 1.0
C A:LYS176 4.0 27.6 1.0
CB A:TYR177 4.1 18.8 1.0
CA A:TYR177 4.2 21.0 1.0
CG A:TYR177 4.4 18.1 1.0
O A:TYR177 4.6 24.5 1.0
O A:HOH465 4.6 26.0 1.0
CE2 A:TYR177 4.7 21.6 1.0
O A:HOH541 4.9 27.5 1.0
O A:GLY175 4.9 38.7 1.0
C A:TYR177 4.9 22.1 1.0
CG A:LYS176 5.0 44.8 1.0

Reference:

A.Laganowsky, M.Zhao, A.B.Soriaga, M.R.Sawaya, D.Cascio, T.O.Yeates. An Approach to Crystallizing Proteins By Metal-Mediated Synthetic Symmetrization. Protein Sci. V. 20 1876 2011.
ISSN: ISSN 0961-8368
PubMed: 21898649
DOI: 10.1002/PRO.727
Page generated: Sat Dec 12 10:09:46 2020

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