Sodium in PDB 3bax: N298S Variant of Human Pancreatic Alpha-Amylase in Complex with Azide

All present enzymatic activity of N298S Variant of Human Pancreatic Alpha-Amylase in Complex with Azide:
3.2.1.1;

The structure of N298S Variant of Human Pancreatic Alpha-Amylase in Complex with Azide, PDB code: 3bax was solved by R.Maurus, G.D.Brayer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	52.070, 67.840, 130.120, 90.00, 90.00, 90.00
R / Rfree (%)	15.5 / 19

The structure of N298S Variant of Human Pancreatic Alpha-Amylase in Complex with Azide also contains other interesting chemical elements:

Chlorine	(Cl)	1 atom
Calcium	(Ca)	1 atom

The binding sites of Sodium atom in the N298S Variant of Human Pancreatic Alpha-Amylase in Complex with Azide (pdb code 3bax). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 3 binding sites of Sodium where determined in the N298S Variant of Human Pancreatic Alpha-Amylase in Complex with Azide, PDB code: 3bax:
Jump to Sodium binding site number: 1; 2; 3;

Sodium binding site 1 out of 3 in the N298S Variant of Human Pancreatic Alpha-Amylase in Complex with Azide


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of N298S Variant of Human Pancreatic Alpha-Amylase in Complex with Azide within 5.0Å range: probe atom residue distance (Å) B Occ A:Na502 b:20.8 occ:1.00 OE1 A:GLU233 2.6 17.2 1.0 O A:HOH608 2.7 23.5 1.0 O A:HOH724 2.7 39.0 1.0 O A:HOH620 2.7 41.1 1.0 O A:HOH1106 2.7 35.9 1.0 O A:HOH1054 2.8 41.9 1.0 OE2 A:GLU233 2.9 18.7 1.0 CD A:GLU233 3.1 17.1 1.0 OD1 A:ASP197 3.6 9.7 1.0 O A:HOH621 4.2 18.5 1.0 O A:HOH867 4.2 33.4 1.0 OD2 A:ASP300 4.3 28.1 1.0 N A:ALA198 4.3 10.0 1.0 CG A:ASP197 4.4 9.0 1.0 O A:HOH612 4.4 26.9 1.0 NH2 A:ARG195 4.5 9.1 1.0 O A:HOH873 4.5 36.4 1.0 O A:HOH560 4.5 69.2 1.0 CA A:ALA198 4.6 10.7 1.0 CG A:GLU233 4.6 15.3 1.0 OD2 A:ASP197 4.6 9.4 1.0 CB A:ALA198 4.7 9.1 1.0 N1 A:AZI500 4.8 26.1 1.0 O A:HOH823 5.0 32.5 1.0

Sodium binding site 2 out of 3 in the N298S Variant of Human Pancreatic Alpha-Amylase in Complex with Azide


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of N298S Variant of Human Pancreatic Alpha-Amylase in Complex with Azide within 5.0Å range: probe atom residue distance (Å) B Occ A:Na503 b:61.9 occ:1.00 O A:HOH861 3.8 60.4 1.0 O A:HOH659 4.0 45.4 1.0 O A:HOH589 4.3 35.5 1.0 O A:THR6 4.4 24.2 1.0 O A:HOH1026 4.7 33.2 1.0 O A:HOH795 4.7 49.1 1.0 NE2 A:GLN8 5.0 45.9 1.0

Sodium binding site 3 out of 3 in the N298S Variant of Human Pancreatic Alpha-Amylase in Complex with Azide


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 3 of N298S Variant of Human Pancreatic Alpha-Amylase in Complex with Azide within 5.0Å range: probe atom residue distance (Å) B Occ A:Na504 b:72.0 occ:1.00 CD A:LYS227 3.1 28.7 1.0 NZ A:LYS227 3.8 34.4 1.0 OE A:PCA1 3.9 23.6 1.0 CE A:LYS227 4.0 31.8 1.0 CG A:LYS227 4.2 24.1 1.0 O A:HOH1058 5.0 36.5 1.0 CD A:PCA1 5.0 20.3 1.0

R.Maurus, A.Begum, L.K.Williams, J.R.Fredriksen, R.Zhang, S.G.Withers, G.D.Brayer. Alternative Catalytic Anions Differentially Modulate Human Alpha-Amylase Activity and Specificity Biochemistry V. 47 3332 2008.
ISSN: ISSN 0006-2960
PubMed: 18284212
DOI: 10.1021/BI701652T