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Sodium in PDB 5iar: Caspase 3 V266W

Enzymatic activity of Caspase 3 V266W

All present enzymatic activity of Caspase 3 V266W:
3.4.22.56;

Protein crystallography data

The structure of Caspase 3 V266W, PDB code: 5iar 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) 31.78 / 1.76
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 68.871, 84.628, 96.237, 90.00, 90.00, 90.00
R / Rfree (%) 15.9 / 18.5

Sodium Binding Sites:

The binding sites of Sodium atom in the Caspase 3 V266W (pdb code 5iar). 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 V266W, PDB code: 5iar:

Sodium binding site 1 out of 1 in 5iar

Go back to Sodium Binding Sites List in 5iar
Sodium binding site 1 out of 1 in the Caspase 3 V266W


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Caspase 3 V266W within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na301

b:19.6
occ:1.00
OE1 A:GLN161 2.7 13.6 1.0
O A:TRP206 2.8 12.2 1.0
N A:PHE215 3.0 11.5 1.0
NE2 A:GLN261 3.0 16.5 1.0
OG A:SER205 3.2 16.8 1.0
CB A:PHE215 3.3 10.0 1.0
CD A:GLN161 3.4 12.4 1.0
N A:TRP214 3.4 11.6 1.0
NE2 A:GLN161 3.5 12.9 1.0
CB A:SER213 3.7 13.9 1.0
CA A:PHE215 3.7 11.8 1.0
CB A:TRP214 3.8 12.3 1.0
CD A:GLN261 3.9 15.6 1.0
C A:TRP214 3.9 12.0 1.0
CA A:TRP214 3.9 11.4 1.0
C A:TRP206 3.9 11.2 1.0
N A:TRP206 3.9 12.8 1.0
OE1 A:GLN261 4.0 14.8 1.0
C A:SER213 4.1 14.0 1.0
OG A:SER213 4.1 11.8 1.0
CB A:SER198 4.2 11.7 1.0
CA A:SER213 4.3 12.7 1.0
CA A:TRP206 4.4 10.8 1.0
OG A:SER198 4.5 11.6 1.0
CB A:SER205 4.5 10.7 1.0
CG A:TRP214 4.6 14.1 1.0
CG A:PHE215 4.6 10.6 1.0
C A:SER205 4.7 13.0 1.0
O A:SER198 4.8 11.2 1.0
N A:ILE216 4.8 11.2 1.0
CG A:GLN161 4.8 13.1 1.0
C A:PHE215 4.8 10.2 1.0
O A:SER213 4.9 12.2 1.0
CA A:SER205 4.9 13.2 1.0
CB A:TRP206 5.0 9.9 1.0

Reference:

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
Page generated: Mon Oct 7 21:34:07 2024

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