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

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

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

Chlorine

(Cl)

1 atom

The binding sites of Copper 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 Copper atom.
In total 2 binding sites of Copper where determined in the Cu-Mediated Dimer of Maltose-Binding Protein A216H/K220H By Synthetic Symmetrization, PDB code: 3ses:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Cu-Mediated Dimer of Maltose-Binding Protein A216H/K220H By Synthetic Symmetrization


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu 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:Cu373 b:26.4 occ:0.63 O A:HIS40 2.1 11.6 1.0 ND1 A:HIS40 2.2 14.4 1.0 OE2 C:GLU222 2.2 17.0 1.0 O C:HOH423 2.2 12.4 1.0 O A:HOH440 2.2 13.2 1.0 NE2 C:HIS216 2.2 16.6 1.0 CE1 A:HIS40 3.1 16.7 1.0 CD C:GLU222 3.2 18.9 1.0 CD2 C:HIS216 3.2 18.0 1.0 CG A:HIS40 3.2 16.7 1.0 C A:HIS40 3.2 14.1 1.0 CE1 C:HIS216 3.3 20.5 1.0 OE1 C:GLU222 3.5 14.6 1.0 CB A:HIS40 3.5 14.9 1.0 CA A:HIS40 3.9 13.3 1.0 O C:HOH374 3.9 16.5 1.0 NE2 A:HIS40 4.2 19.5 1.0 CD2 A:HIS40 4.3 18.0 1.0 O A:HOH419 4.3 18.2 1.0 O A:HOH406 4.3 20.4 1.0 N A:PRO41 4.3 16.5 1.0 CG C:HIS216 4.3 16.8 1.0 ND1 C:HIS216 4.3 17.8 1.0 CG C:GLU222 4.5 16.0 1.0 CA A:PRO41 4.5 18.8 1.0 C A:PRO41 4.6 19.2 1.0 N A:HIS40 4.6 14.8 1.0 OD1 A:ASP42 4.8 31.1 1.0 N A:ASP42 4.9 17.8 1.0 O A:PRO41 4.9 19.7 1.0 O C:HOH391 4.9 23.3 1.0

Copper binding site 2 out of 2 in the Cu-Mediated Dimer of Maltose-Binding Protein A216H/K220H By Synthetic Symmetrization


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 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:Cu374 b:29.5 occ:0.62 O C:HIS40 2.0 16.2 1.0 O C:HOH424 2.2 13.7 1.0 O A:HOH439 2.2 13.4 1.0 OE2 A:GLU222 2.2 17.2 1.0 ND1 C:HIS40 2.3 15.3 1.0 NE2 A:HIS216 2.3 15.5 1.0 CD2 A:HIS216 3.1 14.7 1.0 CD A:GLU222 3.2 17.5 1.0 C C:HIS40 3.2 17.3 1.0 CE1 C:HIS40 3.2 16.7 1.0 CG C:HIS40 3.3 19.6 1.0 CE1 A:HIS216 3.4 18.6 1.0 OE1 A:GLU222 3.4 16.6 1.0 CB C:HIS40 3.6 15.8 1.0 CA C:HIS40 3.9 16.4 1.0 O A:HOH402 4.2 15.1 1.0 O C:HOH408 4.2 20.2 1.0 O C:HOH412 4.2 24.5 1.0 N C:PRO41 4.2 20.0 1.0 CG A:HIS216 4.3 15.0 1.0 NE2 C:HIS40 4.4 16.9 1.0 ND1 A:HIS216 4.4 17.7 1.0 CD2 C:HIS40 4.4 19.5 1.0 C C:PRO41 4.4 21.2 1.0 CA C:PRO41 4.5 21.5 1.0 CG A:GLU222 4.5 14.0 1.0 N C:HIS40 4.7 17.0 1.0 N C:ASP42 4.7 23.9 1.0 O C:PRO41 4.7 17.7 1.0 CA C:GLY14 4.9 23.1 1.0 O A:HOH557 4.9 27.9 1.0 OD1 C:ASP42 5.0 44.0 1.0

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