Zinc in PDB 3sev: Zn-Mediated Trimer of Maltose-Binding Protein E310H/K314H By Synthetic Symmetrization

The structure of Zn-Mediated Trimer of Maltose-Binding Protein E310H/K314H By Synthetic Symmetrization, PDB code: 3sev 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)	39.06 / 3.05
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	113.780, 115.720, 119.450, 90.00, 90.00, 90.00
R / Rfree (%)	22.1 / 26.3

The structure of Zn-Mediated Trimer of Maltose-Binding Protein E310H/K314H By Synthetic Symmetrization also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Zinc atom in the Zn-Mediated Trimer of Maltose-Binding Protein E310H/K314H By Synthetic Symmetrization (pdb code 3sev). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Zn-Mediated Trimer of Maltose-Binding Protein E310H/K314H By Synthetic Symmetrization, PDB code: 3sev:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in the Zn-Mediated Trimer of Maltose-Binding Protein E310H/K314H By Synthetic Symmetrization


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Zn-Mediated Trimer of Maltose-Binding Protein E310H/K314H By Synthetic Symmetrization within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn373 b:41.6 occ:1.00 OE2 C:GLU289 1.9 51.7 1.0 OE1 C:GLU292 1.9 51.8 1.0 ND1 A:HIS310 1.9 34.8 1.0 NE2 A:HIS314 2.1 43.7 1.0 CD C:GLU289 2.8 63.8 1.0 CD C:GLU292 2.8 59.4 1.0 CG A:HIS310 2.9 33.4 1.0 CE1 A:HIS310 3.0 33.7 1.0 CE1 A:HIS314 3.0 43.4 1.0 OE1 C:GLU289 3.1 33.7 1.0 OE2 C:GLU292 3.1 51.8 1.0 CD2 A:HIS314 3.1 43.7 1.0 CB A:HIS310 3.2 31.2 1.0 CA A:HIS310 3.8 31.8 1.0 CD2 A:HIS310 4.1 34.2 1.0 NE2 A:HIS310 4.1 33.9 1.0 CG C:GLU292 4.1 46.2 1.0 CG C:GLU289 4.1 47.4 1.0 ND1 A:HIS314 4.2 43.7 1.0 CG A:HIS314 4.2 42.1 1.0 CB C:GLU292 4.5 39.5 1.0 N A:HIS310 4.7 31.9 1.0 CA C:GLU289 4.7 38.7 1.0 CB A:ALA313 4.8 38.9 1.0 C A:HIS310 5.0 41.3 1.0

Zinc binding site 2 out of 3 in the Zn-Mediated Trimer of Maltose-Binding Protein E310H/K314H By Synthetic Symmetrization


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Zn-Mediated Trimer of Maltose-Binding Protein E310H/K314H By Synthetic Symmetrization within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn373 b:54.9 occ:1.00 OE1 E:GLU292 1.9 77.0 1.0 ND1 C:HIS310 2.0 52.2 1.0 NE2 C:HIS314 2.0 47.6 1.0 OE2 E:GLU289 2.1 29.6 1.0 CD E:GLU292 2.7 70.9 1.0 CE1 C:HIS314 2.9 47.3 1.0 CD E:GLU289 2.9 58.1 1.0 CE1 C:HIS310 3.0 51.8 1.0 OE2 E:GLU292 3.0 49.3 1.0 CG C:HIS310 3.0 50.2 1.0 CD2 C:HIS314 3.0 48.0 1.0 OE1 E:GLU289 3.1 47.2 1.0 CB C:HIS310 3.4 46.4 1.0 CA C:HIS310 3.6 45.4 1.0 ND1 C:HIS314 4.1 48.0 1.0 CG E:GLU292 4.1 58.8 1.0 NE2 C:HIS310 4.1 52.1 1.0 CG C:HIS314 4.1 46.1 1.0 CD2 C:HIS310 4.1 52.2 1.0 O C:HIS310 4.2 51.9 1.0 CG E:GLU289 4.3 56.4 1.0 C C:HIS310 4.4 50.1 1.0 CB C:ALA313 4.6 40.5 1.0 CB E:GLU292 4.6 48.3 1.0 N C:HIS310 4.6 45.8 1.0 CA E:GLU289 4.9 48.2 1.0

Zinc binding site 3 out of 3 in the Zn-Mediated Trimer of Maltose-Binding Protein E310H/K314H By Synthetic Symmetrization


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Zn-Mediated Trimer of Maltose-Binding Protein E310H/K314H By Synthetic Symmetrization within 5.0Å range: probe atom residue distance (Å) B Occ E:Zn373 b:72.0 occ:1.00 OE1 A:GLU289 2.0 54.0 1.0 NE2 E:HIS314 2.1 58.3 1.0 OE1 A:GLU292 2.1 52.0 1.0 ND1 E:HIS310 2.1 58.9 1.0 CD A:GLU289 2.7 71.4 1.0 OE2 A:GLU289 2.9 72.5 1.0 CE1 E:HIS314 2.9 58.0 1.0 CD A:GLU292 3.0 70.1 1.0 CE1 E:HIS310 3.1 58.3 1.0 CG E:HIS310 3.1 57.4 1.0 CD2 E:HIS314 3.2 58.7 1.0 OE2 A:GLU292 3.3 71.7 1.0 CB E:HIS310 3.5 54.6 1.0 CA E:HIS310 3.8 54.5 1.0 ND1 E:HIS314 4.1 58.9 1.0 CG A:GLU289 4.2 54.5 1.0 NE2 E:HIS310 4.2 58.7 1.0 CG E:HIS314 4.3 57.4 1.0 CD2 E:HIS310 4.3 59.0 1.0 CG A:GLU292 4.3 53.4 1.0 O E:HIS310 4.4 57.9 1.0 C E:HIS310 4.6 57.6 1.0 CB E:ALA313 4.7 55.0 1.0 CB A:GLU292 4.7 44.2 1.0 N E:HIS310 4.8 55.5 1.0 CA A:GLU289 4.8 44.9 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