Magnesium in PDB 3sjh: Crystal Structure of A Chimera Containing the N-Terminal Domain (Residues 8-29) of Drosophila Ciboulot and the C-Terminal Domain (Residues 18-44) of Bovine Thymosin-BETA4, Bound to G-Actin-Atp- Latrunculin A

The structure of Crystal Structure of A Chimera Containing the N-Terminal Domain (Residues 8-29) of Drosophila Ciboulot and the C-Terminal Domain (Residues 18-44) of Bovine Thymosin-BETA4, Bound to G-Actin-Atp- Latrunculin A, PDB code: 3sjh 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)	26.88 / 1.75
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	67.644, 74.977, 86.393, 90.00, 90.00, 90.00
R / Rfree (%)	16.9 / 19.9

The binding sites of Magnesium atom in the Crystal Structure of A Chimera Containing the N-Terminal Domain (Residues 8-29) of Drosophila Ciboulot and the C-Terminal Domain (Residues 18-44) of Bovine Thymosin-BETA4, Bound to G-Actin-Atp- Latrunculin A (pdb code 3sjh). 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 of A Chimera Containing the N-Terminal Domain (Residues 8-29) of Drosophila Ciboulot and the C-Terminal Domain (Residues 18-44) of Bovine Thymosin-BETA4, Bound to G-Actin-Atp- Latrunculin A, PDB code: 3sjh:

Magnesium binding site 1 out of 1 in the Crystal Structure of A Chimera Containing the N-Terminal Domain (Residues 8-29) of Drosophila Ciboulot and the C-Terminal Domain (Residues 18-44) of Bovine Thymosin-BETA4, Bound to G-Actin-Atp- Latrunculin A


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of A Chimera Containing the N-Terminal Domain (Residues 8-29) of Drosophila Ciboulot and the C-Terminal Domain (Residues 18-44) of Bovine Thymosin-BETA4, Bound to G-Actin-Atp- Latrunculin A within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg502 b:8.6 occ:1.00 O A:HOH378 1.9 8.1 1.0 O A:HOH379 2.0 10.3 1.0 O2G A:ATP501 2.1 9.0 1.0 O A:HOH377 2.2 16.4 1.0 O1B A:ATP501 2.3 10.9 1.0 O A:HOH376 2.4 15.2 1.0 PG A:ATP501 3.3 11.3 1.0 PB A:ATP501 3.5 9.1 1.0 O A:HOH609 3.6 28.1 1.0 O A:HOH380 3.6 22.7 1.0 O3B A:ATP501 3.8 7.3 1.0 O3G A:ATP501 3.9 11.1 1.0 OE1 A:GLN137 4.0 10.3 1.0 O A:HOH382 4.0 12.7 1.0 CD A:GLN137 4.3 11.7 1.0 O3A A:ATP501 4.3 8.2 1.0 O A:HOH383 4.3 24.7 1.0 CA A:GLY13 4.4 10.1 1.0 O1A A:ATP501 4.4 10.0 1.0 O A:HOH386 4.4 19.9 1.0 NZ A:LYS18 4.4 10.3 1.0 OD2 A:ASP154 4.5 16.5 1.0 OD2 A:ASP11 4.5 10.7 1.0 OD1 A:ASP11 4.5 12.5 1.0 O1G A:ATP501 4.6 11.2 1.0 O2B A:ATP501 4.7 10.8 1.0 NE2 A:GLN137 4.8 10.5 1.0 CG A:GLN137 4.8 9.9 1.0 PA A:ATP501 4.8 10.3 1.0 CG A:ASP11 4.9 10.2 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