Calcium in PDB 4h0t: Crystal Structure of Ia-Adpr-Actin Complex

All present enzymatic activity of Crystal Structure of Ia-Adpr-Actin Complex:
2.4.2.31;

The structure of Crystal Structure of Ia-Adpr-Actin Complex, PDB code: 4h0t was solved by T.Tsurumura, M.Oda, M.Nagahama, H.Tsuge, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.54 / 2.20
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	54.016, 134.169, 151.028, 90.00, 90.00, 90.00
R / Rfree (%)	21.2 / 24

The binding sites of Calcium atom in the Crystal Structure of Ia-Adpr-Actin Complex (pdb code 4h0t). 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 Crystal Structure of Ia-Adpr-Actin Complex, PDB code: 4h0t:

Calcium binding site 1 out of 1 in the Crystal Structure of Ia-Adpr-Actin Complex


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of Ia-Adpr-Actin Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca402 b:21.7 occ:1.00 O B:HOH521 2.2 22.3 1.0 O1B B:ATP404 2.2 20.4 1.0 O B:HOH524 2.2 18.6 1.0 O3G B:ATP404 2.3 20.3 1.0 O B:HOH522 2.4 20.8 1.0 O B:HOH525 2.4 21.9 1.0 O B:HOH526 2.7 23.0 1.0 PG B:ATP404 3.5 20.4 1.0 PB B:ATP404 3.5 20.5 1.0 O1G B:ATP404 3.9 20.3 1.0 O3B B:ATP404 3.9 20.3 1.0 OE1 B:GLN137 4.1 23.4 1.0 O3A B:ATP404 4.2 20.7 1.0 O2A B:ATP404 4.3 20.6 1.0 O B:HOH527 4.3 23.7 1.0 NZ B:LYS18 4.3 22.0 1.0 CA B:GLY13 4.4 22.1 1.0 CD B:GLN137 4.5 23.2 1.0 O B:HOH518 4.5 24.1 1.0 OD1 B:ASP154 4.6 22.1 1.0 OD2 B:ASP11 4.7 20.0 1.0 O B:HOH523 4.7 43.7 1.0 PA B:ATP404 4.7 20.8 1.0 OD1 B:ASP11 4.7 20.1 1.0 OD2 B:ASP154 4.8 23.1 1.0 O2G B:ATP404 4.8 20.3 1.0 O2B B:ATP404 4.8 20.6 1.0 NE2 B:GLN137 4.9 23.5 1.0

T.Tsurumura, Y.Tsumori, H.Qiu, M.Oda, J.Sakurai, M.Nagahama, H.Tsuge. Arginine Adp-Ribosylation Mechanism Based on Structural Snapshots of Iota-Toxin and Actin Complex Proc.Natl.Acad.Sci.Usa V. 110 4267 2013.
ISSN: ISSN 0027-8424
PubMed: 23382240
DOI: 10.1073/PNAS.1217227110