Sodium in PDB 4quj: Caspase-3 T140GV266H

All present enzymatic activity of Caspase-3 T140GV266H:
3.4.22.56;

The structure of Caspase-3 T140GV266H, PDB code: 4quj was solved by C.Cade, P.D.Swartz, S.H.Mackenzie, A.C.Clark, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.78 / 1.50
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	68.363, 84.936, 96.304, 90.00, 90.00, 90.00
R / Rfree (%)	16 / 18.3

The binding sites of Sodium atom in the Caspase-3 T140GV266H (pdb code 4quj). 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 T140GV266H, PDB code: 4quj:

Sodium binding site 1 out of 1 in the Caspase-3 T140GV266H


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Caspase-3 T140GV266H within 5.0Å range: probe atom residue distance (Å) B Occ A:Na301 b:16.9 occ:1.00 OE1 A:GLN161 2.7 11.3 1.0 O A:TRP206 2.8 11.4 1.0 NE2 A:GLN261 3.0 10.8 1.0 N A:PHE215 3.0 10.7 1.0 OG A:SER205 3.3 11.2 0.7 CB A:PHE215 3.3 9.5 1.0 N A:TRP214 3.4 9.8 1.0 CD A:GLN161 3.5 11.7 1.0 NE2 A:GLN161 3.5 13.6 1.0 CB A:SER213 3.7 13.2 1.0 CA A:PHE215 3.7 9.8 1.0 CB A:TRP214 3.8 10.6 1.0 C A:TRP206 3.9 9.1 1.0 CD A:GLN261 3.9 10.4 1.0 CA A:TRP214 3.9 9.6 1.0 C A:TRP214 3.9 10.3 1.0 OE1 A:GLN261 3.9 13.0 1.0 N A:TRP206 4.0 9.1 1.0 C A:SER213 4.1 10.5 1.0 OG A:SER213 4.1 12.4 1.0 CB A:SER198 4.1 10.7 1.0 CA A:SER213 4.3 10.9 1.0 CA A:TRP206 4.4 10.2 1.0 CG A:TRP214 4.6 10.0 1.0 CB A:SER205 4.6 10.4 0.7 CB A:SER205 4.6 10.5 0.3 OG A:SER198 4.6 12.5 1.0 CG A:PHE215 4.7 9.0 1.0 C A:SER205 4.7 9.1 1.0 O A:SER198 4.8 10.8 1.0 N A:ILE216 4.9 9.0 1.0 C A:PHE215 4.9 8.4 1.0 CG A:GLN161 4.9 10.5 1.0 O A:SER213 4.9 10.8 1.0 CB A:TRP206 5.0 10.1 1.0 CA A:SER205 5.0 9.7 0.3 N A:ARG207 5.0 10.9 1.0 CA A:SER205 5.0 9.7 0.7

C.Cade, P.Swartz, S.H.Mackenzie, A.C.Clark. Modifying Caspase-3 Activity By Altering Allosteric Networks. Biochemistry 2014.
ISSN: ISSN 0006-2960
PubMed: 25343534
DOI: 10.1021/BI500874K