Calcium in PDB 2oan: Structure of Oxidized Beta-Actin

The structure of Structure of Oxidized Beta-Actin, PDB code: 2oan was solved by F.Schmitzberger, I.Lassing, P.Nordlund, U.Lindberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.98 / 2.61
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	119.174, 222.589, 133.719, 90.00, 90.00, 90.00
R / Rfree (%)	21 / 28.8

The binding sites of Calcium atom in the Structure of Oxidized Beta-Actin (pdb code 2oan). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 4 binding sites of Calcium where determined in the Structure of Oxidized Beta-Actin, PDB code: 2oan:
Jump to Calcium binding site number: 1; 2; 3; 4;

Calcium binding site 1 out of 4 in the Structure of Oxidized Beta-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 Oxidized Beta-Actin within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca601 b:31.8 occ:1.00 O1B A:ATP501 2.2 26.5 1.0 O A:HOH801 2.3 31.0 1.0 O A:HOH803 2.4 31.4 1.0 O A:HOH802 2.4 31.4 1.0 O A:HOH804 2.4 31.0 1.0 O1G A:ATP501 2.6 25.5 1.0 PB A:ATP501 3.6 28.7 1.0 PG A:ATP501 3.6 27.6 1.0 O3G A:ATP501 3.6 30.5 1.0 CA A:GLY13 4.0 26.4 1.0 O3B A:ATP501 4.0 28.3 1.0 OE1 A:GLN137 4.1 24.4 1.0 O A:ASN12 4.2 26.0 1.0 O3A A:ATP501 4.2 28.3 1.0 O A:HOH890 4.3 25.3 1.0 NZ A:LYS18 4.3 25.6 1.0 CD A:GLN137 4.3 25.0 1.0 OD1 A:ASP11 4.6 24.0 1.0 NE2 A:GLN137 4.6 24.2 1.0 OD2 A:ASP11 4.6 23.7 1.0 O2B A:ATP501 4.8 27.0 1.0 O1A A:ATP501 4.9 28.6 1.0 OD2 A:ASP154 4.9 30.2 1.0 N A:SER14 4.9 29.2 1.0 N A:GLY13 4.9 26.0 1.0 C A:ASN12 4.9 25.5 1.0 PA A:ATP501 5.0 29.4 1.0 CG A:ASP11 5.0 23.7 1.0 C A:GLY13 5.0 28.1 1.0 O2G A:ATP501 5.0 26.6 1.0

Calcium binding site 2 out of 4 in the Structure of Oxidized Beta-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 Oxidized Beta-Actin within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca601 b:43.2 occ:1.00 O B:HOH801 2.3 44.0 1.0 O B:HOH804 2.3 43.2 1.0 O B:HOH802 2.3 43.5 1.0 O B:HOH803 2.4 42.3 1.0 O1B B:ATP501 2.4 35.4 1.0 O1G B:ATP501 3.2 38.6 1.0 O3G B:ATP501 3.3 37.2 1.0 PB B:ATP501 3.4 33.2 1.0 O3A B:ATP501 3.5 33.6 1.0 PG B:ATP501 3.6 37.4 1.0 O3B B:ATP501 3.9 36.0 1.0 NZ B:LYS18 4.2 26.4 1.0 O1A B:ATP501 4.4 31.1 1.0 OD2 B:ASP154 4.5 32.0 1.0 OE1 B:GLN137 4.5 25.6 1.0 PA B:ATP501 4.5 32.5 1.0 CA B:GLY13 4.5 27.5 1.0 OD1 B:ASP154 4.7 32.6 1.0 OD2 B:ASP11 4.7 25.5 1.0 CD B:GLN137 4.8 26.9 1.0 O2B B:ATP501 4.8 33.3 1.0 O B:ASN12 4.8 27.7 1.0 OD1 B:ASP11 4.9 26.1 1.0

Calcium binding site 3 out of 4 in the Structure of Oxidized Beta-Actin


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of Structure of Oxidized Beta-Actin within 5.0Å range: probe atom residue distance (Å) B Occ C:Ca601 b:56.0 occ:1.00 O1B C:ATP501 2.3 39.0 1.0 O1G C:ATP501 3.0 41.7 1.0 PB C:ATP501 3.7 36.9 1.0 O3G C:ATP501 3.9 42.4 1.0 PG C:ATP501 3.9 41.7 1.0 NZ C:LYS18 4.2 32.1 1.0 O3B C:ATP501 4.2 40.5 1.0 O1A C:ATP501 4.3 37.6 1.0 OE1 C:GLN137 4.3 31.8 1.0 O3A C:ATP501 4.4 37.9 1.0 OD2 C:ASP11 4.5 30.6 1.0 OD2 C:ASP154 4.5 36.5 1.0 OD1 C:ASP154 4.5 37.7 1.0 CD C:GLN137 4.5 31.1 1.0 OD1 C:ASP11 4.6 31.3 1.0 CA C:GLY13 4.6 33.2 1.0 PA C:ATP501 4.6 39.0 1.0 O C:ASN12 4.7 32.8 1.0 O2B C:ATP501 4.8 37.0 1.0 O2A C:ATP501 4.8 40.4 1.0 NE2 C:GLN137 4.9 29.0 1.0 CG2 C:VAL339 4.9 31.6 1.0 CG C:ASP11 4.9 30.6 1.0 CG C:ASP154 5.0 35.4 1.0

Calcium binding site 4 out of 4 in the Structure of Oxidized Beta-Actin


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 4 of Structure of Oxidized Beta-Actin within 5.0Å range: probe atom residue distance (Å) B Occ D:Ca601 b:54.3 occ:1.00 O1B D:ATP501 2.3 32.9 1.0 O1G D:ATP501 2.4 31.2 1.0 PG D:ATP501 3.6 34.1 1.0 PB D:ATP501 3.6 31.8 1.0 O3B D:ATP501 4.0 33.1 1.0 O3G D:ATP501 4.0 33.1 1.0 O3A D:ATP501 4.1 31.4 1.0 O D:HOH755 4.2 21.2 1.0 NZ D:LYS18 4.2 30.2 1.0 O1A D:ATP501 4.3 30.8 1.0 OE1 D:GLN137 4.3 29.0 1.0 CA D:GLY13 4.4 30.2 1.0 O D:ASN12 4.5 30.0 1.0 OD2 D:ASP154 4.5 32.1 1.0 CD D:GLN137 4.5 28.7 1.0 OD1 D:ASP11 4.6 28.7 1.0 PA D:ATP501 4.6 28.1 1.0 OD2 D:ASP11 4.6 28.6 1.0 OD1 D:ASP154 4.9 31.8 1.0 NE2 D:GLN137 4.9 26.2 1.0 O2B D:ATP501 4.9 30.6 1.0 O2A D:ATP501 4.9 30.9 1.0 O2G D:ATP501 4.9 31.6 1.0

I.Lassing, F.Schmitzberger, M.Bjornstedt, A.Holmgren, P.Nordlund, C.E.Schutt, U.Lindberg. Molecular and Structural Basis For Redox Regulation of Beta-Actin. J.Mol.Biol. V. 370 331 2007.
ISSN: ISSN 0022-2836
PubMed: 17521670
DOI: 10.1016/J.JMB.2007.04.056