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Sodium in PDB 1e40: Tris/Maltotriose Complex of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 2.2A

Enzymatic activity of Tris/Maltotriose Complex of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 2.2A

All present enzymatic activity of Tris/Maltotriose Complex of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 2.2A:
3.2.1.1;

Protein crystallography data

The structure of Tris/Maltotriose Complex of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 2.2A, PDB code: 1e40 was solved by A.M.Brzozowski, D.M.Lawson, J.P.Turkenburg, H.Bisgaard-Frantzen, A.Svendsen, T.V.Borchert, Z.Dauter, K.S.Wilson, G.J.Davies, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.20
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 52.720, 78.270, 238.860, 90.00, 90.00, 90.00
R / Rfree (%) 13 / 21

Other elements in 1e40:

The structure of Tris/Maltotriose Complex of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 2.2A also contains other interesting chemical elements:

Calcium (Ca) 4 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Tris/Maltotriose Complex of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 2.2A (pdb code 1e40). 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 Tris/Maltotriose Complex of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 2.2A, PDB code: 1e40:

Sodium binding site 1 out of 1 in 1e40

Go back to Sodium Binding Sites List in 1e40
Sodium binding site 1 out of 1 in the Tris/Maltotriose Complex of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 2.2A


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Tris/Maltotriose Complex of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 2.2A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na505

b:9.1
occ:1.00
 OD2 A:ASP159 2.3 5.7 1.0
OD2 A:ASP194 2.3 7.5 1.0
OD2 A:ASP200 2.3 6.0 1.0
O A:VAL201 2.6 5.6 1.0
OD2 A:ASP183 2.6 7.1 1.0
OD1 A:ASP194 2.9 7.3 1.0
CG A:ASP194 3.0 8.6 1.0
CG A:ASP183 3.3 8.3 1.0
CG A:ASP159 3.3 6.8 1.0
CG A:ASP200 3.5 6.4 1.0
C A:VAL201 3.6 6.5 1.0
O A:HOH2151 3.7 8.1 1.0
CB A:ASP159 3.7 5.0 1.0
O A:HOH2275 3.8 7.9 1.0
OD1 A:ASP183 3.8 8.1 1.0
CA A:ASP202 3.9 6.7 1.0
CA A:CA501 4.1 8.1 1.0
CB A:ASP183 4.1 7.7 1.0
N A:ASP202 4.2 5.8 1.0
OD1 A:ASP200 4.2 7.0 1.0
N A:ASP183 4.3 9.2 1.0
N A:TYR203 4.3 6.0 1.0
CB A:ASP194 4.4 7.1 1.0
CA A:CA502 4.4 8.3 1.0
OD1 A:ASP159 4.4 8.0 1.0
O A:ASP200 4.6 6.5 1.0
CB A:ASP200 4.6 5.9 1.0
C A:ASP200 4.6 6.5 1.0
C A:ASP202 4.7 7.2 1.0
N A:VAL201 4.7 6.2 1.0
CA A:VAL201 4.8 6.6 1.0
CA A:ASP183 4.9 8.4 1.0
N A:ASP159 4.9 7.6 1.0
OD1 A:ASP202 4.9 6.1 1.0
CA A:ASP159 4.9 7.0 1.0
CE3 A:TRP182 5.0 8.0 1.0
CB A:ASP202 5.0 7.1 1.0

Reference:

A.M.Brzozowski, D.M.Lawson, J.P.Turkenburg, H.Bisgaard-Frantzen, A.Svendsen, T.V.Borchert, Z.Dauter, K.S.Wilson, G.J.Davies. Structural Analysis of A Chimeric Bacterial Alpha-Amylase. High Resolution Analysis of Native and Ligand Complexes Biochemistry V. 39 9099 2000.
ISSN: ISSN 0006-2960
PubMed: 10924103
DOI: 10.1021/BI0000317
Page generated: Sun Oct 6 18:20:19 2024

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