Calcium in PDB 2v51: Structure of Mal-RPEL1 Complexed to Actin

The structure of Structure of Mal-RPEL1 Complexed to Actin, PDB code: 2v51 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)	20.00 / 2.35
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	53.092, 59.071, 166.203, 90.00, 90.06, 90.00
R / Rfree (%)	18.3 / 24.8

The binding sites of Calcium atom in the Structure of Mal-RPEL1 Complexed to Actin (pdb code 2v51). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Structure of Mal-RPEL1 Complexed to Actin, PDB code: 2v51:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Structure of Mal-RPEL1 Complexed to Actin


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of Mal-RPEL1 Complexed to Actin within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca1373 b:39.5 occ:1.00 O1B B:ATP1372 2.1 32.4 1.0 O B:HOH2038 2.2 17.7 1.0 O B:HOH2002 2.2 24.8 1.0 O1G B:ATP1372 2.3 32.7 1.0 O B:HOH2003 2.4 31.5 1.0 O B:HOH2102 2.4 22.7 1.0 PB B:ATP1372 3.2 33.8 1.0 PG B:ATP1372 3.4 36.9 1.0 O3B B:ATP1372 3.6 32.5 1.0 O B:HOH2093 3.9 20.6 1.0 O3A B:ATP1372 4.0 33.4 1.0 O B:HOH2103 4.1 29.1 1.0 O3G B:ATP1372 4.1 32.8 1.0 O B:HOH2101 4.1 8.0 1.0 O2A B:ATP1372 4.1 30.4 1.0 OD1 B:ASP11 4.3 33.6 1.0 OD2 B:ASP11 4.4 31.0 1.0 O2B B:ATP1372 4.4 33.0 1.0 CA B:GLY13 4.5 34.8 1.0 NZ B:LYS18 4.5 40.2 1.0 PA B:ATP1372 4.5 34.1 1.0 OE1 B:GLN137 4.5 33.8 1.0 OD2 B:ASP154 4.5 42.8 1.0 O2G B:ATP1372 4.6 34.5 1.0 OD1 B:ASP154 4.6 35.6 1.0 CD B:GLN137 4.6 35.5 1.0 CG B:ASP11 4.8 36.4 1.0 O1A B:ATP1372 4.8 36.7 1.0 CA B:GLY156 4.9 32.5 1.0

Calcium binding site 2 out of 2 in the Structure of Mal-RPEL1 Complexed to Actin


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Structure of Mal-RPEL1 Complexed to Actin within 5.0Å range: probe atom residue distance (Å) B Occ D:Ca1373 b:41.6 occ:1.00 O1B D:ATP1372 2.1 34.6 1.0 O1G D:ATP1372 2.2 35.5 1.0 O D:HOH2004 2.2 25.6 1.0 O D:HOH2042 2.2 20.8 1.0 O D:HOH2003 2.3 27.7 1.0 O D:HOH2049 2.4 24.7 1.0 PB D:ATP1372 3.2 33.3 1.0 PG D:ATP1372 3.3 37.6 1.0 O3B D:ATP1372 3.5 36.2 1.0 O D:HOH2093 3.9 25.8 1.0 O D:HOH2096 4.0 20.6 1.0 O3G D:ATP1372 4.0 32.4 1.0 O D:HOH2095 4.0 7.0 1.0 O3A D:ATP1372 4.0 34.6 1.0 O2A D:ATP1372 4.0 35.0 1.0 O D:HOH2043 4.2 43.8 1.0 O2B D:ATP1372 4.4 33.3 1.0 OD1 D:ASP11 4.4 36.5 1.0 OD2 D:ASP154 4.4 44.4 1.0 O2G D:ATP1372 4.5 32.5 1.0 OD1 D:ASP154 4.5 35.2 1.0 OE1 D:GLN137 4.5 33.7 1.0 PA D:ATP1372 4.5 36.9 1.0 NZ D:LYS18 4.6 29.0 1.0 CA D:GLY13 4.6 35.4 1.0 CD D:GLN137 4.6 32.5 1.0 OD2 D:ASP11 4.7 32.7 1.0 CA D:GLY156 4.8 32.0 1.0 CG D:ASP154 4.9 36.4 1.0 O1A D:ATP1372 4.9 33.9 1.0 NE2 D:GLN137 5.0 27.9 1.0 CG D:ASP11 5.0 34.5 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