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Sodium in PDB 5i9b: Caspase 3 V266A

Enzymatic activity of Caspase 3 V266A

All present enzymatic activity of Caspase 3 V266A:
3.4.22.56;

Protein crystallography data

The structure of Caspase 3 V266A, PDB code: 5i9b 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) 27.91 / 1.80
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 68.556, 84.545, 96.146, 90.00, 90.00, 90.00
R / Rfree (%) 16.7 / 20.4

Sodium Binding Sites:

The binding sites of Sodium atom in the Caspase 3 V266A (pdb code 5i9b). 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 V266A, PDB code: 5i9b:

Sodium binding site 1 out of 1 in 5i9b

Go back to Sodium Binding Sites List in 5i9b
Sodium binding site 1 out of 1 in the Caspase 3 V266A


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Caspase 3 V266A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na301

b:17.9
occ:1.00
OE1 A:GLN161 2.7 11.7 1.0
O A:TRP206 2.7 11.1 1.0
N A:PHE215 3.0 7.4 1.0
NE2 A:GLN261 3.0 15.4 1.0
OG A:SER205 3.2 13.9 1.0
CB A:PHE215 3.3 8.1 1.0
CD A:GLN161 3.4 13.7 1.0
N A:TRP214 3.4 7.6 1.0
NE2 A:GLN161 3.6 13.7 1.0
CB A:SER213 3.7 12.3 1.0
CA A:PHE215 3.7 7.8 1.0
C A:TRP206 3.9 12.5 1.0
CB A:TRP214 3.9 10.0 1.0
C A:TRP214 3.9 8.9 1.0
CA A:TRP214 3.9 9.7 1.0
CD A:GLN261 3.9 13.4 1.0
N A:TRP206 4.0 8.9 1.0
OG A:SER213 4.0 10.6 1.0
C A:SER213 4.0 12.5 1.0
OE1 A:GLN261 4.1 17.4 1.0
CB A:SER198 4.1 8.9 1.0
CA A:SER213 4.3 9.8 1.0
CA A:TRP206 4.4 10.6 1.0
OG A:SER198 4.5 9.7 1.0
CB A:SER205 4.6 10.2 1.0
CG A:PHE215 4.6 7.9 1.0
CG A:TRP214 4.7 8.1 1.0
C A:SER205 4.7 13.7 1.0
O A:SER198 4.7 8.1 1.0
N A:ILE216 4.8 9.8 1.0
CG A:GLN161 4.8 9.5 1.0
C A:PHE215 4.8 8.2 1.0
O A:SER213 4.9 10.9 1.0
N A:ARG207 5.0 10.9 1.0
CA A:SER205 5.0 10.1 1.0
CB A:TRP206 5.0 7.5 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 Aug 18 00:13:55 2025

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