Magnesium in PDB 3u9z: Crystal Structure Between Actin and A Protein Construct Containing the First Beta-Thymosin Domain of Drosophila Ciboulot (Residues 2-58) with the Three Mutations N26D/Q27K/D28S

The structure of Crystal Structure Between Actin and A Protein Construct Containing the First Beta-Thymosin Domain of Drosophila Ciboulot (Residues 2-58) with the Three Mutations N26D/Q27K/D28S, PDB code: 3u9z was solved by L.Renault, C.Husson, M.F.Carlier, D.Didry, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.00 / 2.09
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	45.795, 75.181, 117.708, 90.00, 90.00, 90.00
R / Rfree (%)	16 / 22.7

The binding sites of Magnesium atom in the Crystal Structure Between Actin and A Protein Construct Containing the First Beta-Thymosin Domain of Drosophila Ciboulot (Residues 2-58) with the Three Mutations N26D/Q27K/D28S (pdb code 3u9z). 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 Crystal Structure Between Actin and A Protein Construct Containing the First Beta-Thymosin Domain of Drosophila Ciboulot (Residues 2-58) with the Three Mutations N26D/Q27K/D28S, PDB code: 3u9z:

Magnesium binding site 1 out of 1 in the Crystal Structure Between Actin and A Protein Construct Containing the First Beta-Thymosin Domain of Drosophila Ciboulot (Residues 2-58) with the Three Mutations N26D/Q27K/D28S


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure Between Actin and A Protein Construct Containing the First Beta-Thymosin Domain of Drosophila Ciboulot (Residues 2-58) with the Three Mutations N26D/Q27K/D28S within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg377 b:17.3 occ:1.00 O A:HOH670 2.0 12.8 1.0 O3B A:ADP376 2.1 17.1 1.0 O A:HOH635 2.1 6.7 1.0 O A:HOH430 2.2 5.0 1.0 O A:HOH428 2.3 10.5 1.0 PB A:ADP376 3.4 14.3 1.0 O1B A:ADP376 3.8 12.2 1.0 O A:HOH452 3.9 21.0 1.0 O A:HOH441 3.9 20.0 1.0 O1A A:ADP376 4.0 14.1 1.0 O3A A:ADP376 4.2 13.7 1.0 NE2 A:GLN137 4.2 11.0 1.0 NZ A:LYS18 4.2 16.6 1.0 O A:HOH416 4.2 9.2 1.0 OD1 A:ASP154 4.2 16.1 1.0 OD1 A:ASP11 4.3 14.4 1.0 OD2 A:ASP154 4.3 19.9 1.0 OD2 A:ASP11 4.4 18.1 1.0 PA A:ADP376 4.5 15.4 1.0 O2B A:ADP376 4.5 13.2 1.0 CA A:GLY13 4.6 15.9 1.0 CD A:GLN137 4.6 15.5 1.0 CG2 A:VAL339 4.7 14.3 1.0 CG A:ASP154 4.7 15.8 1.0 CG A:ASP11 4.8 17.5 1.0 O2A A:ADP376 4.9 15.6 1.0 CG A:GLN137 5.0 12.6 1.0 CE A:LYS18 5.0 12.4 1.0 CA A:GLY156 5.0 12.3 1.0

D.Didry, F.X.Cantrelle, C.Husson, P.Roblin, A.M.Moorthy, J.Perez, C.Le Clainche, M.Hertzog, E.Guittet, M.F.Carlier, C.Van Heijenoort, L.Renault. How A Single Residue in Individual Beta-Thymosin/WH2 Domains Controls Their Functions in Actin Assembly Embo J. V. 31 1000 2012.
ISSN: ISSN 0261-4189
PubMed: 22193718
DOI: 10.1038/EMBOJ.2011.461