Magnesium in PDB 2v52: Structure of Mal-RPEL2 Complexed to G-Actin

The structure of Structure of Mal-RPEL2 Complexed to G-Actin, PDB code: 2v52 was solved by S.Mouilleron, S.Guettler, C.A.Langer, R.Treisman, N.Q.Mcdonald, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.35 / 1.45
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	54.750, 55.440, 138.390, 90.00, 90.00, 90.00
R / Rfree (%)	14.7 / 18.8

The binding sites of Magnesium atom in the Structure of Mal-RPEL2 Complexed to G-Actin (pdb code 2v52). 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 Structure of Mal-RPEL2 Complexed to G-Actin, PDB code: 2v52:

Magnesium binding site 1 out of 1 in the Structure of Mal-RPEL2 Complexed to G-Actin


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Mal-RPEL2 Complexed to G-Actin within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg403 b:13.2 occ:1.00 O B:HOH686 2.1 15.1 1.0 O B:HOH552 2.1 13.3 1.0 O1B B:ATP402 2.1 12.5 1.0 O1G B:ATP402 2.1 11.5 0.8 O B:HOH575 2.1 13.4 1.0 O B:HOH574 2.2 14.7 1.0 PB B:ATP402 3.3 12.6 1.0 PG B:ATP402 3.4 12.1 0.8 O3B B:ATP402 3.6 13.2 1.0 O B:HOH528 3.7 20.9 1.0 O B:HOH560 3.7 18.3 1.0 O B:HOH644 4.1 17.8 1.0 O3G B:ATP402 4.1 14.1 0.8 O3A B:ATP402 4.1 12.1 1.0 O2A B:ATP402 4.1 13.8 1.0 OE1 B:GLN137 4.1 13.9 1.0 O B:HOH553 4.2 20.1 1.0 NZ B:LYS18 4.2 13.0 1.0 OD1 B:ASP11 4.4 14.0 1.0 CA B:GLY13 4.5 13.7 1.0 OD2 B:ASP11 4.5 14.3 1.0 OD1 B:ASP154 4.5 19.1 1.0 O2G B:ATP402 4.5 12.8 0.8 O2B B:ATP402 4.6 12.9 1.0 CD B:GLN137 4.6 13.0 1.0 PA B:ATP402 4.6 13.2 1.0 CG B:ASP11 4.8 13.4 1.0 CA B:GLY156 4.9 10.9 1.0

S.Mouilleron, S.Guettler, C.A.Langer, R.Treisman, N.Q.Mcdonald. Molecular Basis For G-Actin Binding to Rpel Motifs From the Serum Response Factor Coactivator Mal. Embo J. V. 27 3198 2008.
ISSN: ESSN 1460-2075
PubMed: 19008859
DOI: 10.1038/EMBOJ.2008.235