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Sodium in PDB 1e3z: Acarbose Complex of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 1.93A

Enzymatic activity of Acarbose Complex of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 1.93A

All present enzymatic activity of Acarbose Complex of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 1.93A:
3.2.1.1;

Protein crystallography data

The structure of Acarbose Complex of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 1.93A, PDB code: 1e3z 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 / 1.93
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 / 20

Other elements in 1e3z:

The structure of Acarbose Complex of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 1.93A also contains other interesting chemical elements:

Calcium (Ca) 4 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Acarbose Complex of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 1.93A (pdb code 1e3z). 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 Acarbose Complex of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 1.93A, PDB code: 1e3z:

Sodium binding site 1 out of 1 in 1e3z

Go back to Sodium Binding Sites List in 1e3z
Sodium binding site 1 out of 1 in the Acarbose Complex of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 1.93A


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Acarbose Complex of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 1.93A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na505

b:5.4
occ:1.00
 OD2 A:ASP200 2.3 6.3 1.0
OD2 A:ASP159 2.3 5.3 1.0
OD2 A:ASP194 2.4 6.7 1.0
OD2 A:ASP183 2.5 7.4 1.0
O A:VAL201 2.6 4.6 1.0
OD1 A:ASP194 2.8 7.6 1.0
CG A:ASP194 2.9 7.7 1.0
CG A:ASP183 3.2 7.9 1.0
CG A:ASP159 3.4 5.9 1.0
CG A:ASP200 3.5 6.9 1.0
C A:VAL201 3.6 5.2 1.0
O A:HOH2341 3.6 6.7 1.0
O A:HOH2317 3.7 4.6 1.0
CB A:ASP159 3.7 5.4 1.0
OD1 A:ASP183 3.7 6.0 1.0
CA A:ASP202 4.0 5.1 1.0
CA A:CA501 4.0 5.7 1.0
CB A:ASP183 4.1 7.4 1.0
OD1 A:ASP200 4.2 5.3 1.0
N A:ASP202 4.2 3.7 1.0
N A:ASP183 4.4 6.5 1.0
CB A:ASP194 4.4 6.2 1.0
N A:TYR203 4.4 5.8 1.0
OD1 A:ASP159 4.5 5.0 1.0
CA A:CA502 4.5 6.4 1.0
CB A:ASP200 4.6 5.1 1.0
O A:ASP200 4.6 6.0 1.0
C A:ASP200 4.7 5.2 1.0
N A:VAL201 4.7 5.2 1.0
C A:ASP202 4.7 5.5 1.0
CA A:VAL201 4.8 5.1 1.0
CA A:ASP183 4.9 7.6 1.0
CE3 A:TRP182 4.9 6.1 1.0
CB A:ASP202 5.0 4.8 1.0
N A:ASP159 5.0 5.6 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 18:20:09 2024

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