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Sodium in PDB 1ob0: Kinetic Stabilization of Bacillus Licheniformis Alpha-Amylase Through Introduction of Hydrophobic Residues at the Surface
Enzymatic activity of Kinetic Stabilization of Bacillus Licheniformis Alpha-Amylase Through Introduction of Hydrophobic Residues at the Surface
All present enzymatic activity of Kinetic Stabilization of Bacillus Licheniformis Alpha-Amylase Through Introduction of Hydrophobic Residues at the Surface:
3.2.1.1;
3.2.1.1;
Protein crystallography data
The structure of Kinetic Stabilization of Bacillus Licheniformis Alpha-Amylase Through Introduction of Hydrophobic Residues at the Surface, PDB code: 1ob0
was solved by
M.Machius,
N.Declerck,
R.Huber,
G.Wiegand,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
| Resolution Low / High (Å) | 25.89 / 1.83 |
| Space group | P 61 |
| Cell size a, b, c (Å), α, β, γ (°) | 91.292, 91.292, 137.466, 90.00, 90.00, 120.00 |
| R / Rfree (%) | 14.7 / 15.4 |
Other elements in 1ob0:
The structure of Kinetic Stabilization of Bacillus Licheniformis Alpha-Amylase Through Introduction of Hydrophobic Residues at the Surface also contains other interesting chemical elements:
| Calcium | (Ca) | 3 atoms |
Sodium Binding Sites:
The binding sites of Sodium atom in the Kinetic Stabilization of Bacillus Licheniformis Alpha-Amylase Through Introduction of Hydrophobic Residues at the Surface
(pdb code 1ob0). 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 Kinetic Stabilization of Bacillus Licheniformis Alpha-Amylase Through Introduction of Hydrophobic Residues at the Surface, PDB code: 1ob0:
In total only one binding site of Sodium was determined in the Kinetic Stabilization of Bacillus Licheniformis Alpha-Amylase Through Introduction of Hydrophobic Residues at the Surface, PDB code: 1ob0:
Sodium binding site 1 out of 1 in 1ob0
Go back to
Sodium Binding Sites List in 1ob0
Sodium binding site 1 out
of 1 in the Kinetic Stabilization of Bacillus Licheniformis Alpha-Amylase Through Introduction of Hydrophobic Residues at the Surface
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Sodium with other atoms in the Na binding
site number 1 of Kinetic Stabilization of Bacillus Licheniformis Alpha-Amylase Through Introduction of Hydrophobic Residues at the Surface within 5.0Å range:
|
Reference:
M.Machius,
N.Declerck,
R.Huber,
G.Wiegand.
Kinetic Stabilization of Bacillus Licheniformis Alpha-Amylase Through Introduction of Hydrophobic Residues at the Surface J.Biol.Chem. V. 278 11546 2003.
ISSN: ISSN 0021-9258
PubMed: 12540849
DOI: 10.1074/JBC.M212618200
Page generated: Tue Dec 15 05:32:14 2020
ISSN: ISSN 0021-9258
PubMed: 12540849
DOI: 10.1074/JBC.M212618200
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