Zinc in PDB 3ser: Zn-Mediated Polymer of Maltose-Binding Protein K26H/K30H By Synthetic Symmetrization

The structure of Zn-Mediated Polymer of Maltose-Binding Protein K26H/K30H By Synthetic Symmetrization, PDB code: 3ser 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)	64.15 / 2.35
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	57.700, 116.370, 65.040, 90.00, 99.47, 90.00
R / Rfree (%)	18.1 / 22.2

The structure of Zn-Mediated Polymer of Maltose-Binding Protein K26H/K30H By Synthetic Symmetrization also contains other interesting chemical elements:

Chlorine	(Cl)	3 atoms
Calcium	(Ca)	1 atom

The binding sites of Zinc atom in the Zn-Mediated Polymer of Maltose-Binding Protein K26H/K30H By Synthetic Symmetrization (pdb code 3ser). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Zn-Mediated Polymer of Maltose-Binding Protein K26H/K30H By Synthetic Symmetrization, PDB code: 3ser:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Zn-Mediated Polymer of Maltose-Binding Protein K26H/K30H 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 Polymer of Maltose-Binding Protein K26H/K30H By Synthetic Symmetrization within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn373 b:24.9 occ:1.00 NE2 C:HIS26 2.2 23.1 1.0 NE2 C:HIS30 2.2 25.8 1.0 O C:HOH401 2.4 28.1 1.0 CE1 C:HIS26 3.1 21.6 1.0 CD2 C:HIS26 3.2 23.3 1.0 CE1 C:HIS30 3.2 25.1 1.0 CD2 C:HIS30 3.2 24.4 1.0 ND1 C:HIS26 4.2 25.9 1.0 ND1 C:HIS30 4.3 24.3 1.0 CG C:HIS26 4.3 22.1 1.0 CG C:HIS30 4.3 24.3 1.0

Zinc binding site 2 out of 2 in the Zn-Mediated Polymer of Maltose-Binding Protein K26H/K30H 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 Polymer of Maltose-Binding Protein K26H/K30H By Synthetic Symmetrization within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn374 b:25.7 occ:1.00 OD2 C:ASP165 2.2 36.4 1.0 CL C:CL375 2.5 50.9 1.0 OD1 C:ASP165 2.8 23.2 1.0 CG C:ASP165 2.8 28.9 1.0 CD C:LYS252 3.6 33.7 1.0 CE C:LYS252 4.1 36.5 1.0 CB C:ASP165 4.3 26.6 1.0 O C:ASP165 4.5 24.4 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