Zinc in PDB 3sew: Zn-Mediated Polymer of Maltose-Binding Protein A216H/K220H By Synthetic Symmetrization (Form I)

The structure of Zn-Mediated Polymer of Maltose-Binding Protein A216H/K220H By Synthetic Symmetrization (Form I), PDB code: 3sew 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)	66.38 / 1.55
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	85.580, 63.440, 66.390, 90.00, 90.75, 90.00
R / Rfree (%)	16.1 / 18.8

The structure of Zn-Mediated Polymer of Maltose-Binding Protein A216H/K220H By Synthetic Symmetrization (Form I) also contains other interesting chemical elements:

Chlorine

(Cl)

4 atoms

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

Zinc binding site 1 out of 1 in the Zn-Mediated Polymer of Maltose-Binding Protein A216H/K220H By Synthetic Symmetrization (Form I)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Zn-Mediated Polymer of Maltose-Binding Protein A216H/K220H By Synthetic Symmetrization (Form I) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn373 b:16.4 occ:1.00 NE2 A:HIS216 2.0 16.6 1.0 OE1 A:GLU222 2.1 16.1 1.0 CL A:CL376 2.2 16.4 1.0 CD A:GLU222 2.9 17.9 1.0 OE2 A:GLU222 3.0 16.8 1.0 CD2 A:HIS216 3.0 13.9 1.0 CE1 A:HIS216 3.1 15.8 1.0 O A:HOH650 4.1 32.3 1.0 ND1 A:HIS216 4.2 12.7 1.0 CG A:HIS216 4.2 13.0 1.0 O A:HOH470 4.2 29.9 1.0 CG A:GLU222 4.3 13.7 1.0 CB A:HIS220 4.9 16.6 1.0 CG A:HIS220 5.0 19.7 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