Sodium in PDB 5ian: Caspase 3 V266N

All present enzymatic activity of Caspase 3 V266N:
3.4.22.56;

The structure of Caspase 3 V266N, PDB code: 5ian was solved by J.J.Maciag, S.H.Mackenzie, M.B.Tucker, J.L.Schipper, P.D.Swartz, A.C.Clark, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.86 / 2.70
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	69.021, 84.910, 96.386, 90.00, 90.00, 90.00
R / Rfree (%)	16.3 / 24.7

The binding sites of Sodium atom in the Caspase 3 V266N (pdb code 5ian). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Caspase 3 V266N, PDB code: 5ian:

Sodium binding site 1 out of 1 in the Caspase 3 V266N


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Caspase 3 V266N within 5.0Å range: probe atom residue distance (Å) B Occ A:Na301 b:19.6 occ:1.00 O A:TRP206 2.6 11.9 1.0 OE1 A:GLN161 2.7 24.8 1.0 NE2 A:GLN161 3.0 22.4 1.0 NE2 A:GLN261 3.2 20.7 1.0 OG A:SER205 3.2 17.4 1.0 CD A:GLN161 3.2 16.6 1.0 N A:PHE215 3.3 11.8 1.0 CB A:PHE215 3.5 9.2 1.0 OE1 A:GLN261 3.6 13.5 1.0 C A:TRP206 3.7 14.8 1.0 N A:TRP206 3.7 16.5 1.0 N A:TRP214 3.7 11.3 1.0 CB A:SER213 3.8 9.1 1.0 CD A:GLN261 3.8 10.1 1.0 CA A:PHE215 4.0 15.6 1.0 CB A:TRP214 4.2 9.7 1.0 C A:SER213 4.2 15.3 1.0 OG A:SER213 4.2 11.7 1.0 CB A:SER198 4.2 20.2 1.0 C A:TRP214 4.2 17.9 1.0 CA A:TRP206 4.2 10.9 1.0 CA A:TRP214 4.3 7.9 1.0 OG A:SER198 4.3 14.5 1.0 CB A:SER205 4.3 13.8 1.0 CA A:SER213 4.4 13.9 1.0 C A:SER205 4.5 17.1 1.0 CA A:SER205 4.7 10.3 1.0 CG A:GLN161 4.7 19.0 1.0 O A:SER198 4.7 13.5 1.0 CG A:PHE215 4.8 8.0 1.0 CG A:TRP214 4.8 16.1 1.0 N A:ARG207 4.8 24.8 1.0 CB A:TRP206 4.8 8.6 1.0 O A:SER213 5.0 29.9 1.0

J.J.Maciag, S.H.Mackenzie, M.B.Tucker, J.L.Schipper, P.Swartz, A.C.Clark. Tunable Allosteric Library of Caspase-3 Identifies Coupling Between Conserved Water Molecules and Conformational Selection. Proc.Natl.Acad.Sci.Usa V. 113 E6080 2016.
ISSN: ESSN 1091-6490
PubMed: 27681633
DOI: 10.1073/PNAS.1603549113