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Sodium in PDB 1e43: Native Structure of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 1.7A

Enzymatic activity of Native Structure of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 1.7A

All present enzymatic activity of Native Structure of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 1.7A:
3.2.1.1;

Protein crystallography data

The structure of Native Structure of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 1.7A, PDB code: 1e43 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 / 1.70
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 52.200, 76.100, 236.500, 90.00, 90.00, 90.00
R / Rfree (%) 13.3 / 18.5

Other elements in 1e43:

The structure of Native Structure of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 1.7A also contains other interesting chemical elements:

Calcium (Ca) 4 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Native Structure of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 1.7A (pdb code 1e43). 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 Native Structure of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 1.7A, PDB code: 1e43:

Sodium binding site 1 out of 1 in 1e43

Go back to Sodium Binding Sites List in 1e43
Sodium binding site 1 out of 1 in the Native Structure of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 1.7A


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Native Structure of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 1.7A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na505

b:4.9
occ:1.00
 OD2 A:ASP194 2.3 5.7 1.0
OD2 A:ASP159 2.3 5.2 1.0
OD2 A:ASP200 2.4 7.0 1.0
O A:VAL201 2.4 4.9 1.0
OD2 A:ASP183 2.5 6.1 1.0
OD1 A:ASP194 2.9 5.6 1.0
CG A:ASP194 2.9 6.1 1.0
CG A:ASP183 3.2 6.1 1.0
CG A:ASP159 3.3 3.9 1.0
C A:VAL201 3.5 4.5 1.0
CG A:ASP200 3.5 6.0 1.0
O A:HOH2341 3.6 6.9 1.0
CB A:ASP159 3.7 4.8 1.0
O A:HOH2534 3.8 6.7 1.0
OD1 A:ASP183 3.8 6.7 1.0
CA A:ASP202 3.8 5.0 1.0
CB A:ASP183 3.9 6.0 1.0
N A:ASP202 4.0 4.2 1.0
CA A:CA501 4.0 5.3 1.0
OD1 A:ASP200 4.1 5.9 1.0
N A:ASP183 4.3 5.3 1.0
N A:TYR203 4.3 5.5 1.0
CB A:ASP194 4.4 5.6 1.0
OD1 A:ASP159 4.5 4.8 1.0
O A:ASP200 4.5 4.1 1.0
CA A:CA502 4.5 5.8 1.0
C A:ASP200 4.5 5.1 1.0
CB A:ASP200 4.6 5.0 1.0
CA A:VAL201 4.6 4.5 1.0
N A:VAL201 4.6 4.8 1.0
C A:ASP202 4.6 5.0 1.0
CA A:ASP183 4.8 5.8 1.0
N A:ASP159 4.8 5.9 1.0
CE3 A:TRP182 4.9 6.5 1.0
CB A:ASP202 4.9 6.2 1.0
CA A:ASP159 4.9 5.4 1.0
OD1 A:ASP202 4.9 5.5 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 18:20:45 2024

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