Sodium in PDB 5iak: Caspase 3 V266S

All present enzymatic activity of Caspase 3 V266S:
3.4.22.56;

The structure of Caspase 3 V266S, PDB code: 5iak 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)	23.32 / 1.82
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	68.725, 84.485, 96.302, 90.00, 90.00, 90.00
R / Rfree (%)	15.8 / 19.9

The binding sites of Sodium atom in the Caspase 3 V266S (pdb code 5iak). 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 V266S, PDB code: 5iak:

Sodium binding site 1 out of 1 in the Caspase 3 V266S


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Caspase 3 V266S within 5.0Å range: probe atom residue distance (Å) B Occ A:Na301 b:12.7 occ:1.00 OE1 A:GLN161 2.7 10.0 1.0 O A:TRP206 2.8 7.9 1.0 NE2 A:GLN261 2.9 10.4 1.0 N A:PHE215 3.1 7.2 1.0 OG A:SER205 3.1 8.6 1.0 CB A:PHE215 3.3 4.8 1.0 CD A:GLN161 3.4 6.5 1.0 NE2 A:GLN161 3.5 9.8 1.0 N A:TRP214 3.5 5.7 1.0 CB A:SER213 3.7 9.0 1.0 CA A:PHE215 3.8 6.3 1.0 C A:TRP206 3.9 8.2 1.0 CD A:GLN261 3.9 7.6 1.0 N A:TRP206 3.9 8.4 1.0 CB A:TRP214 3.9 7.5 1.0 OE1 A:GLN261 4.0 13.0 1.0 C A:TRP214 4.0 7.3 1.0 CA A:TRP214 4.0 9.4 1.0 C A:SER213 4.1 6.7 1.0 OG A:SER213 4.1 7.8 1.0 CB A:SER198 4.1 5.8 1.0 CA A:SER213 4.3 6.7 1.0 CA A:TRP206 4.4 8.9 1.0 CB A:SER205 4.5 5.9 1.0 OG A:SER198 4.5 8.2 1.0 CG A:PHE215 4.7 7.5 1.0 CG A:TRP214 4.7 7.4 1.0 C A:SER205 4.7 8.6 1.0 CG A:GLN161 4.7 5.8 1.0 O A:SER198 4.8 5.9 1.0 N A:ILE216 4.8 6.2 1.0 C A:PHE215 4.9 4.8 1.0 O A:SER213 4.9 8.1 1.0 CA A:SER205 4.9 7.8 1.0 CB A:TRP206 4.9 4.8 1.0 N A:ARG207 5.0 7.9 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