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Sodium in PDB 1bli: Bacillus Licheniformis Alpha-Amylase

Enzymatic activity of Bacillus Licheniformis Alpha-Amylase

All present enzymatic activity of Bacillus Licheniformis Alpha-Amylase:
3.2.1.1;

Protein crystallography data

The structure of Bacillus Licheniformis Alpha-Amylase, PDB code: 1bli 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) 30.00 / 1.90
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 91.300, 91.300, 137.700, 90.00, 90.00, 120.00
R / Rfree (%) 15.4 / 18.5

Other elements in 1bli:

The structure of Bacillus Licheniformis Alpha-Amylase also contains other interesting chemical elements:

Calcium (Ca) 3 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Bacillus Licheniformis Alpha-Amylase (pdb code 1bli). 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 Bacillus Licheniformis Alpha-Amylase, PDB code: 1bli:

Sodium binding site 1 out of 1 in 1bli

Go back to Sodium Binding Sites List in 1bli
Sodium binding site 1 out of 1 in the Bacillus Licheniformis Alpha-Amylase


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Bacillus Licheniformis Alpha-Amylase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na800

b:17.8
occ:1.00
OD2 A:ASP200 2.4 17.0 1.0
OD2 A:ASP161 2.4 18.7 1.0
OD2 A:ASP194 2.5 17.2 1.0
O A:ILE201 2.5 15.0 1.0
OD2 A:ASP183 2.7 17.7 1.0
OD1 A:ASP194 3.1 16.5 1.0
CG A:ASP194 3.1 17.4 1.0
CG A:ASP183 3.3 15.4 1.0
CG A:ASP161 3.4 18.9 1.0
C A:ILE201 3.5 16.4 1.0
CG A:ASP200 3.6 16.4 1.0
O A:HOH2080 3.6 14.9 1.0
OD1 A:ASP183 3.7 19.1 1.0
CB A:ASP161 3.8 16.2 1.0
CA A:ASP202 3.8 16.9 1.0
O A:HOH1036 3.8 12.6 1.0
N A:ASP202 4.0 15.7 1.0
CA A:CA600 4.1 16.0 1.0
CB A:ASP183 4.2 15.3 1.0
N A:TYR203 4.3 17.7 1.0
O A:ASP200 4.3 15.5 1.0
N A:ASP183 4.4 16.3 1.0
OD1 A:ASP200 4.4 19.0 1.0
C A:ASP200 4.5 15.5 1.0
CA A:CA500 4.5 18.5 1.0
OD1 A:ASP161 4.5 20.2 1.0
CB A:ASP200 4.5 13.6 1.0
CB A:ASP194 4.5 16.8 1.0
N A:ILE201 4.6 14.9 1.0
C A:ASP202 4.6 18.1 1.0
CA A:ILE201 4.6 14.2 1.0
CE3 A:TRP182 4.8 17.6 1.0
CB A:ASP202 4.9 17.4 1.0
N A:ASP161 4.9 17.4 1.0
CA A:ASP183 4.9 17.6 1.0

Reference:

M.Machius, N.Declerck, R.Huber, G.Wiegand. Activation of Bacillus Licheniformis Alpha-Amylase Through A Disorder-->Order Transition of the Substrate-Binding Site Mediated By A Calcium-Sodium-Calcium Metal Triad. Structure V. 6 281 1998.
ISSN: ISSN 0969-2126
PubMed: 9551551
DOI: 10.1016/S0969-2126(98)00032-X
Page generated: Tue Dec 15 05:22:11 2020

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