Calcium in PDB 2aso: Structure of Rabbit Actin in Complex with Sphinxolide B

The structure of Structure of Rabbit Actin in Complex with Sphinxolide B, PDB code: 2aso was solved by J.S.Allingham, A.Zampella, M.V.D'auria, I.Rayment, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.00 / 1.70
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	58.182, 54.989, 103.520, 90.00, 92.41, 90.00
R / Rfree (%)	17.3 / 21.3

The binding sites of Calcium atom in the Structure of Rabbit Actin in Complex with Sphinxolide B (pdb code 2aso). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Structure of Rabbit Actin in Complex with Sphinxolide B, PDB code: 2aso:

Calcium binding site 1 out of 1 in the Structure of Rabbit Actin in Complex with Sphinxolide B


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of Rabbit Actin in Complex with Sphinxolide B within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca400 b:13.9 occ:1.00 O2B A:ATP425 2.2 10.6 1.0 O3G A:ATP425 2.3 10.5 1.0 O A:HOH506 2.4 16.3 1.0 O A:HOH507 2.4 14.7 1.0 O A:HOH508 2.4 16.2 1.0 O A:HOH516 2.4 13.7 1.0 O A:HOH505 2.7 17.2 1.0 PB A:ATP425 3.5 11.1 1.0 PG A:ATP425 3.5 11.9 1.0 O1G A:ATP425 3.9 12.8 1.0 O3B A:ATP425 3.9 11.0 1.0 O3A A:ATP425 4.1 10.9 1.0 OE1 A:GLN137 4.2 15.3 1.0 O A:HOH509 4.2 15.3 1.0 O1A A:ATP425 4.3 12.9 1.0 NZ A:LYS18 4.4 14.5 1.0 CA A:GLY13 4.4 15.5 1.0 CD A:GLN137 4.4 14.7 1.0 O A:HOH576 4.6 19.4 1.0 OD2 A:ASP154 4.6 20.5 1.0 OD1 A:ASP11 4.6 13.2 1.0 OD2 A:ASP11 4.7 14.8 1.0 O1B A:ATP425 4.7 10.4 1.0 PA A:ATP425 4.7 11.9 1.0 O A:HOH517 4.7 28.3 1.0 O2G A:ATP425 4.8 12.3 1.0 NE2 A:GLN137 4.9 14.5 1.0 CG A:GLN137 4.9 14.1 1.0 OD1 A:ASP154 4.9 24.3 1.0

J.S.Allingham, A.Zampella, M.V.D'auria, I.Rayment. Structures of Microfilament Destabilizing Toxins Bound to Actin Provide Insight Into Toxin Design and Activity Proc.Natl.Acad.Sci.Usa V. 102 14527 2005.
ISSN: ISSN 0027-8424
PubMed: 16192358
DOI: 10.1073/PNAS.0502089102