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

Enzymatic activity of 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;

Protein crystallography data

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

Other elements in 3bax:

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

Chlorine (Cl) 1 atom
Sodium (Na) 3 atoms

Calcium Binding Sites:

The binding sites of Calcium 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 Calcium atom.
In total only one binding site of Calcium was determined in the N298S Variant of Human Pancreatic Alpha-Amylase in Complex with Azide, PDB code: 3bax:

Calcium binding site 1 out of 1 in 3bax

Go back to Calcium Binding Sites List in 3bax
Calcium binding site 1 out of 1 in the N298S Variant of Human Pancreatic Alpha-Amylase in Complex with Azide


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca 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:Ca498

b:12.3
occ:1.00
 O A:HIS201 2.5 12.7 1.0
O A:ARG158 2.5 13.0 1.0
OD1 A:ASN100 2.5 10.3 1.0
OD1 A:ASP167 2.6 11.8 1.0
OD2 A:ASP167 2.6 13.0 1.0
O A:HOH891 2.7 12.1 1.0
O A:HOH562 2.7 8.0 1.0
O A:HOH892 2.8 17.3 1.0
CG A:ASP167 3.0 13.0 1.0
C A:ARG158 3.5 12.7 1.0
CG A:ASN100 3.5 11.2 1.0
C A:HIS201 3.6 12.4 1.0
ND2 A:ASN100 3.9 9.3 1.0
CA A:ARG158 4.1 11.9 1.0
CB A:HIS201 4.2 13.4 1.0
O A:ASN100 4.4 11.4 1.0
O A:HOH625 4.4 9.2 1.0
CA A:HIS201 4.5 12.3 1.0
CB A:ASP167 4.5 12.1 1.0
ND2 A:ASN137 4.5 16.2 1.0
N A:MET202 4.6 11.4 1.0
N A:ASP159 4.6 14.0 1.0
O A:CYS160 4.6 12.8 1.0
CA A:MET202 4.6 11.0 1.0
O A:VAL157 4.7 12.8 1.0
CG A:MET202 4.8 9.6 1.0
CA A:ASP159 4.8 13.4 1.0
O A:LEU168 4.8 10.5 1.0
CB A:ASN100 4.9 10.5 1.0
O A:HOH997 4.9 11.6 1.0
CB A:ARG158 5.0 11.4 1.0

Reference:

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
Page generated: Sat Jul 13 08:13:38 2024

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