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Sodium in PDB 1wp6: Crystal Structure of Maltohexaose-Producing Amylase From Alkalophilic Bacillus Sp.707.

Enzymatic activity of Crystal Structure of Maltohexaose-Producing Amylase From Alkalophilic Bacillus Sp.707.

All present enzymatic activity of Crystal Structure of Maltohexaose-Producing Amylase From Alkalophilic Bacillus Sp.707.:
3.2.1.98;

Protein crystallography data

The structure of Crystal Structure of Maltohexaose-Producing Amylase From Alkalophilic Bacillus Sp.707., PDB code: 1wp6 was solved by R.Kanai, K.Haga, T.Akiba, K.Yamane, K.Harata, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 6.00 / 2.10
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 47.620, 82.800, 127.170, 90.00, 90.00, 90.00
R / Rfree (%) 16.6 / 21

Other elements in 1wp6:

The structure of Crystal Structure of Maltohexaose-Producing Amylase From Alkalophilic Bacillus Sp.707. also contains other interesting chemical elements:

Calcium (Ca) 3 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of Maltohexaose-Producing Amylase From Alkalophilic Bacillus Sp.707. (pdb code 1wp6). 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 Crystal Structure of Maltohexaose-Producing Amylase From Alkalophilic Bacillus Sp.707., PDB code: 1wp6:

Sodium binding site 1 out of 1 in 1wp6

Go back to Sodium Binding Sites List in 1wp6
Sodium binding site 1 out of 1 in the Crystal Structure of Maltohexaose-Producing Amylase From Alkalophilic Bacillus Sp.707.


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of Maltohexaose-Producing Amylase From Alkalophilic Bacillus Sp.707. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na504

b:24.5
occ:1.00
 OD2 A:ASP163 2.3 20.1 1.0
OD2 A:ASP199 2.4 18.7 1.0
OD2 A:ASP205 2.5 21.1 1.0
OD2 A:ASP188 2.6 19.2 1.0
O A:ILE206 2.8 19.3 1.0
OD1 A:ASP199 3.1 17.6 1.0
CG A:ASP199 3.1 17.6 1.0
CG A:ASP163 3.3 19.9 1.0
CG A:ASP188 3.3 22.1 1.0
O A:HOH637 3.6 15.3 1.0
CB A:ASP163 3.6 19.2 1.0
CG A:ASP205 3.7 19.5 1.0
C A:ILE206 3.7 19.5 1.0
O A:HOH638 3.8 18.7 1.0
CA A:ASP207 3.9 17.3 1.0
OD1 A:ASP188 4.0 21.8 1.0
CA A:CA502 4.0 17.7 1.0
CB A:ASP188 4.1 18.1 1.0
N A:ASP207 4.2 17.8 1.0
N A:ASP188 4.2 18.9 1.0
O A:ASP205 4.4 17.9 1.0
OD1 A:ASP163 4.4 20.4 1.0
N A:MET208 4.4 18.6 1.0
CA A:CA501 4.4 20.3 1.0
OD1 A:ASP205 4.5 19.9 1.0
CB A:ASP199 4.5 17.1 1.0
CB A:ASP205 4.6 18.5 1.0
C A:ASP205 4.6 18.6 1.0
C A:ASP207 4.8 18.1 1.0
OD1 A:ASP207 4.8 14.8 1.0
CE3 A:TRP187 4.8 16.4 1.0
N A:ILE206 4.8 19.8 1.0
CA A:ASP188 4.8 18.8 1.0
CB A:ASP207 4.8 17.4 1.0
CA A:ILE206 4.9 17.7 1.0
CA A:ASP163 4.9 19.9 1.0
N A:ASP163 4.9 19.5 1.0

Reference:

R.Kanai, K.Haga, T.Akiba, K.Yamane, K.Harata. Biochemical and Crystallographic Analyses of Maltohexaose-Producing Amylase From Alkalophilic Bacillus Sp. 707 Biochemistry V. 43 14047 2004.
ISSN: ISSN 0006-2960
PubMed: 15518553
DOI: 10.1021/BI048489M
Page generated: Mon Oct 7 00:26:45 2024

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