Magnesium in PDB 1qjh: Protein Aggregation and Alzheimer'S Disease: Crystallographic Analysis of the Phenomenon. Engineered Version of the Ribosomal Protein S6 Used As A Stable Scaffold to Study Oligomerization.

The structure of Protein Aggregation and Alzheimer'S Disease: Crystallographic Analysis of the Phenomenon. Engineered Version of the Ribosomal Protein S6 Used As A Stable Scaffold to Study Oligomerization., PDB code: 1qjh was solved by O.Kristensen, D.E.Otzen, M.Oliveberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.00 / 2.20
Space group	P 42 21 2
Cell size a, b, c (Å), α, β, γ (°)	49.701, 49.701, 73.255, 90.00, 90.00, 90.00
R / Rfree (%)	20.5 / 27.5

The binding sites of Magnesium atom in the Protein Aggregation and Alzheimer'S Disease: Crystallographic Analysis of the Phenomenon. Engineered Version of the Ribosomal Protein S6 Used As A Stable Scaffold to Study Oligomerization. (pdb code 1qjh). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Protein Aggregation and Alzheimer'S Disease: Crystallographic Analysis of the Phenomenon. Engineered Version of the Ribosomal Protein S6 Used As A Stable Scaffold to Study Oligomerization., PDB code: 1qjh:

Magnesium binding site 1 out of 1 in the Protein Aggregation and Alzheimer'S Disease: Crystallographic Analysis of the Phenomenon. Engineered Version of the Ribosomal Protein S6 Used As A Stable Scaffold to Study Oligomerization.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Protein Aggregation and Alzheimer'S Disease: Crystallographic Analysis of the Phenomenon. Engineered Version of the Ribosomal Protein S6 Used As A Stable Scaffold to Study Oligomerization. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1000 b:38.7 occ:0.50 O A:HOH2005 2.3 52.7 1.0 O A:HOH2003 2.7 65.8 0.5 O A:HOH2002 3.4 63.6 1.0 O A:HOH2012 4.5 49.4 1.0

D.E.Otzen, O.Kristensen, M.Oliveberg. Designed Protein Tetramer Zipped Together with A Hydrophobic Alzheimer Homology: A Structural Clue to Amyloid Assembly. Proc. Natl. Acad. Sci. V. 97 9907 2000U.S.A..
ISSN: ISSN 0027-8424
PubMed: 10944185
DOI: 10.1073/PNAS.160086297