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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;

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:

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

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:
probe atom residue distance (Å) B Occ
A:Na504

b:19.1
occ:1.00
OD1 A:ASP161 2.4 17.0 1.0
OD2 A:ASP194 2.5 16.6 1.0
OD2 A:ASP200 2.5 18.7 1.0
O A:ILE201 2.6 15.2 1.0
OD2 A:ASP183 2.6 17.6 1.0
OD1 A:ASP194 3.0 15.8 1.0
CG A:ASP194 3.1 17.9 1.0
CG A:ASP183 3.2 19.2 1.0
CG A:ASP161 3.4 19.3 1.0
C A:ILE201 3.6 15.9 1.0
O A:HOH2060 3.6 15.6 1.0
CG A:ASP200 3.7 18.9 1.0
OD1 A:ASP183 3.7 17.8 1.0
O A:HOH2125 3.7 15.3 1.0
CB A:ASP161 3.8 15.8 1.0
CA A:ASP202 3.9 17.2 1.0
CB A:ASP183 4.0 17.6 1.0
CA A:CA501 4.1 15.8 1.0
N A:ASP202 4.1 15.6 1.0
N A:ASP183 4.3 18.7 1.0
N A:TYR203 4.3 17.2 1.0
OD1 A:ASP200 4.4 17.9 1.0
CA A:CA502 4.5 19.5 1.0
O A:ASP200 4.5 15.0 1.0
CB A:ASP194 4.5 15.1 1.0
OD2 A:ASP161 4.5 16.4 1.0
C A:ASP200 4.6 15.0 1.0
CB A:ASP200 4.6 14.4 1.0
C A:ASP202 4.6 17.8 1.0
N A:ILE201 4.6 14.4 1.0
CA A:ILE201 4.7 14.8 1.0
CA A:ASP183 4.8 18.0 1.0
CE3 A:TRP182 4.9 18.7 1.0
CB A:ASP202 5.0 18.3 1.0
N A:ASP161 5.0 16.0 1.0

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: Sun Aug 17 06:52:05 2025

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