Sodium in PDB 5iaj: Caspase 3 V266L

All present enzymatic activity of Caspase 3 V266L:
3.4.22.56;

The structure of Caspase 3 V266L, PDB code: 5iaj 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)	27.15 / 1.58
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	69.375, 84.871, 96.564, 90.00, 90.00, 90.00
R / Rfree (%)	17.8 / 20.3

The binding sites of Sodium atom in the Caspase 3 V266L (pdb code 5iaj). 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 V266L, PDB code: 5iaj:

Sodium binding site 1 out of 1 in the Caspase 3 V266L


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Caspase 3 V266L within 5.0Å range: probe atom residue distance (Å) B Occ A:Na301 b:18.4 occ:1.00 OE1 A:GLN161 2.8 13.5 1.0 O A:TRP206 2.8 13.0 1.0 N A:PHE215 3.0 13.4 1.0 NE2 A:GLN261 3.0 13.6 1.0 OG A:SER205 3.3 13.5 1.0 CB A:PHE215 3.3 11.1 1.0 N A:TRP214 3.4 11.9 1.0 CD A:GLN161 3.5 13.5 1.0 NE2 A:GLN161 3.6 13.7 1.0 CB A:SER213 3.6 13.6 1.0 CA A:PHE215 3.7 13.7 1.0 CB A:TRP214 3.9 13.4 1.0 C A:TRP206 3.9 11.2 1.0 C A:TRP214 3.9 12.5 1.0 CA A:TRP214 3.9 12.2 1.0 CD A:GLN261 3.9 13.6 1.0 N A:TRP206 3.9 11.2 1.0 OE1 A:GLN261 4.0 15.7 1.0 OG A:SER213 4.0 16.3 1.0 C A:SER213 4.0 13.1 1.0 CB A:SER198 4.2 12.6 1.0 CA A:SER213 4.3 12.9 1.0 CA A:TRP206 4.4 13.4 1.0 OG A:SER198 4.6 13.3 1.0 CB A:SER205 4.6 14.6 1.0 CG A:TRP214 4.6 12.0 1.0 CG A:PHE215 4.7 10.1 1.0 C A:SER205 4.7 11.5 1.0 O A:SER198 4.8 12.1 1.0 N A:ILE216 4.8 10.5 1.0 C A:PHE215 4.8 10.2 1.0 O A:SER213 4.9 11.7 1.0 CG A:GLN161 4.9 12.8 1.0 CB A:TRP206 5.0 13.4 1.0 CA A:SER205 5.0 10.9 1.0 N A:ARG207 5.0 12.4 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