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Sodium in PDB 1glh: Cation Binding to A Bacillus (1,3-1,4)-Beta-Glucanase. Geometry, Affinity and Effect on Protein Stability

Enzymatic activity of Cation Binding to A Bacillus (1,3-1,4)-Beta-Glucanase. Geometry, Affinity and Effect on Protein Stability

All present enzymatic activity of Cation Binding to A Bacillus (1,3-1,4)-Beta-Glucanase. Geometry, Affinity and Effect on Protein Stability:
3.2.1.73;

Protein crystallography data

The structure of Cation Binding to A Bacillus (1,3-1,4)-Beta-Glucanase. Geometry, Affinity and Effect on Protein Stability, PDB code: 1glh was solved by T.Keitel, U.Heinemann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 70.220, 72.560, 49.970, 90.00, 90.00, 90.00
R / Rfree (%) n/a / n/a

Sodium Binding Sites:

The binding sites of Sodium atom in the Cation Binding to A Bacillus (1,3-1,4)-Beta-Glucanase. Geometry, Affinity and Effect on Protein Stability (pdb code 1glh). 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 Cation Binding to A Bacillus (1,3-1,4)-Beta-Glucanase. Geometry, Affinity and Effect on Protein Stability, PDB code: 1glh:

Sodium binding site 1 out of 1 in 1glh

Go back to Sodium Binding Sites List in 1glh
Sodium binding site 1 out of 1 in the Cation Binding to A Bacillus (1,3-1,4)-Beta-Glucanase. Geometry, Affinity and Effect on Protein Stability


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Cation Binding to A Bacillus (1,3-1,4)-Beta-Glucanase. Geometry, Affinity and Effect on Protein Stability within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na330

b:13.3
occ:1.00
 O A:ASP207 2.2 13.9 1.0
O A:GLY45 2.2 17.1 1.0
O A:PRO9 2.3 16.2 1.0
OD1 A:ASP207 2.4 8.9 1.0
C A:ASP207 3.2 11.9 1.0
C A:PRO9 3.4 14.7 1.0
CG A:ASP207 3.4 11.3 1.0
C A:GLY45 3.5 16.7 1.0
CA A:ASP207 3.6 12.7 1.0
CB A:ASP207 4.1 9.4 1.0
CA A:PRO9 4.1 14.3 1.0
CA A:GLY45 4.3 20.6 1.0
N A:TRP208 4.4 12.1 1.0
N A:LYS46 4.4 14.3 1.0
N A:PHE10 4.4 13.8 1.0
CA A:LYS46 4.4 10.9 1.0
OD2 A:ASP207 4.4 11.1 1.0
CB A:PHE10 4.5 8.8 1.0
ND2 A:ASN11 4.5 29.4 1.0
CB A:PRO9 4.6 14.4 1.0
O A:TYR206 4.7 10.1 1.0
CA A:PHE10 4.7 14.0 1.0
C A:PHE10 4.7 17.9 1.0
O A:PHE10 4.8 18.5 1.0
CA A:TRP208 4.9 14.7 1.0
CD A:LYS46 4.9 18.6 1.0
N A:ASP207 4.9 10.8 1.0
CD2 A:PHE10 5.0 7.3 1.0
CB A:TRP208 5.0 13.1 1.0

Reference:

T.Keitel, M.Meldgaard, U.Heinemann. Cation Binding to A Bacillus (1,3-1,4)-Beta-Glucanase. Geometry, Affinity and Effect on Protein Stability Eur.J.Biochem. V. 222 203 1994.
ISSN: ISSN 0014-2956
PubMed: 8200344
DOI: 10.1111/J.1432-1033.1994.TB18858.X
Page generated: Sun Aug 17 05:06:06 2025

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