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Sodium in PDB 2gjp: Structure of Bacillus Halmapalus Alpha-Amylase, Crystallized with the Substrate Analogue Acarbose and Maltose

Enzymatic activity of Structure of Bacillus Halmapalus Alpha-Amylase, Crystallized with the Substrate Analogue Acarbose and Maltose

All present enzymatic activity of Structure of Bacillus Halmapalus Alpha-Amylase, Crystallized with the Substrate Analogue Acarbose and Maltose:
3.2.1.1;

Protein crystallography data

The structure of Structure of Bacillus Halmapalus Alpha-Amylase, Crystallized with the Substrate Analogue Acarbose and Maltose, PDB code: 2gjp 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) 14.84 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 46.993, 73.497, 151.094, 90.00, 90.00, 90.00
R / Rfree (%) 17.2 / 21.4

Other elements in 2gjp:

The structure of Structure of Bacillus Halmapalus Alpha-Amylase, Crystallized with the Substrate Analogue Acarbose and Maltose 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, Crystallized with the Substrate Analogue Acarbose and Maltose (pdb code 2gjp). 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, Crystallized with the Substrate Analogue Acarbose and Maltose, PDB code: 2gjp:

Sodium binding site 1 out of 1 in 2gjp

Go back to Sodium Binding Sites List in 2gjp
Sodium binding site 1 out of 1 in the Structure of Bacillus Halmapalus Alpha-Amylase, Crystallized with the Substrate Analogue Acarbose and Maltose


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, Crystallized with the Substrate Analogue Acarbose and Maltose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na1489

b:8.9
occ:1.00
 OD2 A:ASP163 2.3 14.5 1.0
OD2 A:ASP188 2.4 12.1 1.0
OD2 A:ASP205 2.4 14.7 1.0
O A:VAL206 2.5 11.7 1.0
OD2 A:ASP199 2.5 13.1 1.0
OD1 A:ASP199 2.8 12.3 1.0
CG A:ASP199 3.0 12.7 1.0
CG A:ASP188 3.1 11.7 1.0
CG A:ASP163 3.3 12.0 1.0
C A:VAL206 3.5 10.0 1.0
O A:HOH1563 3.5 12.0 1.0
O A:HOH1499 3.6 16.7 1.0
CG A:ASP205 3.6 13.8 1.0
OD1 A:ASP188 3.6 12.7 1.0
CB A:ASP163 3.6 12.2 1.0
CA A:ASP207 3.8 11.4 1.0
CB A:ASP188 4.0 10.6 1.0
CA A:CA1486 4.0 12.3 1.0
N A:ASP207 4.1 8.2 1.0
N A:MET208 4.2 10.7 1.0
N A:ASP188 4.2 11.2 1.0
OD1 A:ASP205 4.3 12.8 1.0
OD1 A:ASP163 4.3 12.6 1.0
CA A:CA1487 4.4 13.0 1.0
CB A:ASP199 4.4 10.2 1.0
O A:ASP205 4.5 12.3 1.0
CB A:ASP205 4.5 12.8 1.0
C A:ASP205 4.6 11.7 1.0
N A:VAL206 4.6 10.1 1.0
C A:ASP207 4.6 11.1 1.0
CA A:VAL206 4.7 9.9 1.0
CA A:ASP188 4.7 10.8 1.0
OD1 A:ASP207 4.8 13.1 1.0
CB A:ASP207 4.9 11.1 1.0
CA A:ASP163 4.9 12.0 1.0
CE3 A:TRP187 4.9 12.8 1.0
N A:ASP163 4.9 10.4 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 02:38:14 2024

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