Sodium in PDB 6bg1: Caspase-3 Mutant - D9A,D28A,S150E

All present enzymatic activity of Caspase-3 Mutant - D9A,D28A,S150E:
3.4.22.56;

The structure of Caspase-3 Mutant - D9A,D28A,S150E, PDB code: 6bg1 was solved by M.E.Thomas, R.Grinshpon, 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)	35.72 / 1.88
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	68.428, 84.476, 96.423, 90.00, 90.00, 90.00
R / Rfree (%)	16.3 / 19.3

The binding sites of Sodium atom in the Caspase-3 Mutant - D9A,D28A,S150E (pdb code 6bg1). 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 Mutant - D9A,D28A,S150E, PDB code: 6bg1:

Sodium binding site 1 out of 1 in the Caspase-3 Mutant - D9A,D28A,S150E


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Caspase-3 Mutant - D9A,D28A,S150E within 5.0Å range: probe atom residue distance (Å) B Occ A:Na301 b:19.2 occ:1.00 O C:TRP206 2.7 14.3 1.0 OE1 A:GLN161 2.8 13.2 1.0 NE2 C:GLN261 3.0 17.6 1.0 N C:PHE215 3.0 13.0 1.0 OG C:SER205 3.2 14.5 1.0 CB C:PHE215 3.3 9.1 1.0 N C:TRP214 3.4 12.4 1.0 CD A:GLN161 3.5 14.4 1.0 CB C:SER213 3.6 16.3 1.0 NE2 A:GLN161 3.7 16.8 1.0 CA C:PHE215 3.8 9.1 1.0 C C:TRP206 3.8 11.4 1.0 CB C:TRP214 3.9 10.4 1.0 C C:TRP214 3.9 11.2 1.0 CD C:GLN261 3.9 18.9 1.0 N C:TRP206 3.9 13.7 1.0 CA C:TRP214 3.9 11.9 1.0 C C:SER213 4.0 15.4 1.0 OG C:SER213 4.1 13.0 1.0 OE1 C:GLN261 4.1 18.3 1.0 CB C:SER198 4.2 12.7 1.0 CA C:SER213 4.2 13.8 1.0 CA C:TRP206 4.4 13.5 1.0 CB C:SER205 4.6 12.5 1.0 OG C:SER198 4.6 16.7 1.0 CG C:TRP214 4.6 11.1 1.0 C C:SER205 4.7 15.7 1.0 CG C:PHE215 4.7 8.8 1.0 O C:SER198 4.8 12.4 1.0 N C:ILE216 4.8 14.2 1.0 C C:PHE215 4.9 11.2 1.0 CG A:GLN161 4.9 12.7 1.0 O C:SER213 4.9 15.2 1.0 CB C:TRP206 4.9 9.6 1.0 N C:ARG207 4.9 15.5 1.0 CA C:SER205 5.0 14.1 1.0

M.E.Thomas, R.Grinshpon, P.Swartz, A.C.Clark. Modifications to A Common Phosphorylation Network Provide Individualized Control in Caspases. J. Biol. Chem. V. 293 5447 2018.
ISSN: ESSN 1083-351X
PubMed: 29414778
DOI: 10.1074/JBC.RA117.000728