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Sodium in PDB 2gjr: Structure of Bacillus Halmapalus Alpha-Amylase Without Any Substrate Analogues

Enzymatic activity of Structure of Bacillus Halmapalus Alpha-Amylase Without Any Substrate Analogues

All present enzymatic activity of Structure of Bacillus Halmapalus Alpha-Amylase Without Any Substrate Analogues:
3.2.1.1;

Protein crystallography data

The structure of Structure of Bacillus Halmapalus Alpha-Amylase Without Any Substrate Analogues, PDB code: 2gjr was solved by L.Lyhne-Iversen, T.J.Hobley, S.G.Kaasgaard, P.Harris, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.95 / 2.10
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 38.550, 59.040, 209.800, 90.00, 90.00, 90.00
R / Rfree (%) 20 / 24.2

Other elements in 2gjr:

The structure of Structure of Bacillus Halmapalus Alpha-Amylase Without Any Substrate Analogues also contains other interesting chemical elements:

Calcium (Ca) 3 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Structure of Bacillus Halmapalus Alpha-Amylase Without Any Substrate Analogues (pdb code 2gjr). 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 Structure of Bacillus Halmapalus Alpha-Amylase Without Any Substrate Analogues, PDB code: 2gjr:

Sodium binding site 1 out of 1 in 2gjr

Go back to Sodium Binding Sites List in 2gjr
Sodium binding site 1 out of 1 in the Structure of Bacillus Halmapalus Alpha-Amylase Without Any Substrate Analogues


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Structure of Bacillus Halmapalus Alpha-Amylase Without Any Substrate Analogues within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na1489

b:10.8
occ:1.00
 OD2 A:ASP188 2.2 10.1 1.0
OD2 A:ASP163 2.3 10.0 1.0
OD2 A:ASP205 2.3 9.4 1.0
OD2 A:ASP199 2.4 11.4 1.0
O A:VAL206 2.5 9.9 1.0
OD1 A:ASP199 2.8 11.1 1.0
CG A:ASP199 3.0 11.2 1.0
CG A:ASP188 3.1 10.3 1.0
CG A:ASP163 3.3 10.4 1.0
CG A:ASP205 3.5 9.6 1.0
C A:VAL206 3.5 11.2 1.0
O A:HOH1524 3.5 8.4 1.0
CB A:ASP163 3.6 10.0 1.0
O A:HOH1512 3.7 18.2 1.0
OD1 A:ASP188 3.8 9.6 1.0
CA A:ASP207 3.9 11.3 1.0
CA A:CA1486 3.9 7.2 1.0
CB A:ASP188 4.0 10.5 1.0
N A:ASP207 4.1 11.5 1.0
OD1 A:ASP205 4.1 8.8 1.0
N A:ASP188 4.2 12.3 1.0
N A:MET208 4.3 10.7 1.0
CA A:CA1487 4.3 15.4 1.0
OD1 A:ASP163 4.4 9.6 1.0
CB A:ASP199 4.4 10.6 1.0
O A:ASP205 4.6 10.6 1.0
N A:VAL206 4.6 10.7 1.0
C A:ASP205 4.6 10.3 1.0
CB A:ASP205 4.6 9.6 1.0
C A:ASP207 4.6 11.5 1.0
CA A:VAL206 4.7 11.1 1.0
CA A:ASP188 4.7 11.4 1.0
N A:ASP163 4.8 9.7 1.0
CA A:ASP163 4.8 9.3 1.0
CB A:ASP207 4.9 12.1 1.0
CE3 A:TRP187 5.0 15.5 1.0
OD1 A:ASP207 5.0 12.6 1.0

Reference:

L.Lyhne-Iversen, T.J.Hobley, S.G.Kaasgaard, P.Harris. Structure of Bacillus Halmapalus Alpha-Amylase Crystallized with and Without the Substrate Analogue Acarbose and Maltose. Acta Crystallogr.,Sect.F V. 62 849 2006.
ISSN: ESSN 1744-3091
PubMed: 16946462
DOI: 10.1107/S174430910603096X
Page generated: Mon Oct 7 02:38:54 2024

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