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

Protein crystallography data

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

Other elements in 3sev:

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

Zinc Binding Sites:

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 3sev

Go back to Zinc Binding Sites List in 3sev
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 3sev

Go back to Zinc Binding Sites List in 3sev
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 3sev

Go back to Zinc Binding Sites List in 3sev
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

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: Wed Dec 16 04:50:03 2020

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