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Calcium in PDB 4x0n: Porcine Pancreatic Alpha-Amylase in Complex with Helianthamide, A Novel Proteinaceous Inhibitor

Enzymatic activity of Porcine Pancreatic Alpha-Amylase in Complex with Helianthamide, A Novel Proteinaceous Inhibitor

All present enzymatic activity of Porcine Pancreatic Alpha-Amylase in Complex with Helianthamide, A Novel Proteinaceous Inhibitor:
3.2.1.1;

Protein crystallography data

The structure of Porcine Pancreatic Alpha-Amylase in Complex with Helianthamide, A Novel Proteinaceous Inhibitor, PDB code: 4x0n was solved by L.K.Williams, G.D.Brayer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.89 / 2.60
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 43.750, 103.280, 111.896, 90.00, 90.00, 90.00
R / Rfree (%) 18.2 / 22.6

Other elements in 4x0n:

The structure of Porcine Pancreatic Alpha-Amylase in Complex with Helianthamide, A Novel Proteinaceous Inhibitor also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the Porcine Pancreatic Alpha-Amylase in Complex with Helianthamide, A Novel Proteinaceous Inhibitor (pdb code 4x0n). 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 Porcine Pancreatic Alpha-Amylase in Complex with Helianthamide, A Novel Proteinaceous Inhibitor, PDB code: 4x0n:

Calcium binding site 1 out of 1 in 4x0n

Go back to Calcium Binding Sites List in 4x0n
Calcium binding site 1 out of 1 in the Porcine Pancreatic Alpha-Amylase in Complex with Helianthamide, A Novel Proteinaceous Inhibitor


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Porcine Pancreatic Alpha-Amylase in Complex with Helianthamide, A Novel Proteinaceous Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca502

b:14.5
occ:1.00
 O A:HOH807 2.3 15.0 1.0
O A:HOH806 2.4 13.4 1.0
OD1 A:ASP167 2.4 14.4 1.0
OD1 A:ASN100 2.4 13.0 1.0
O A:ARG158 2.4 16.2 1.0
O A:HOH805 2.4 8.3 1.0
O A:HIS201 2.5 12.4 1.0
OD2 A:ASP167 2.5 12.4 1.0
CG A:ASP167 2.8 13.2 1.0
CG A:ASN100 3.4 11.6 1.0
C A:ARG158 3.4 15.8 1.0
C A:HIS201 3.7 13.5 1.0
ND2 A:ASN100 3.9 10.1 1.0
CA A:ARG158 4.1 13.8 1.0
O A:ASN100 4.2 12.9 1.0
CB A:ASP167 4.3 13.4 1.0
O A:HOH726 4.3 13.7 1.0
CB A:HIS201 4.4 11.8 1.0
N A:ASP159 4.4 16.3 1.0
CG A:MET202 4.5 14.8 1.0
O A:CYS160 4.5 16.0 1.0
ND2 A:ASN137 4.5 14.2 1.0
N A:MET202 4.6 12.8 1.0
CA A:HIS201 4.6 13.9 1.0
CA A:MET202 4.6 11.1 1.0
CB A:ASN100 4.7 9.9 1.0
O A:VAL157 4.7 15.1 1.0
O A:LEU168 4.7 18.9 1.0
CA A:ASP159 4.7 13.5 1.0
O A:HOH730 4.9 10.6 1.0
CB A:ARG158 4.9 15.0 1.0
CA A:ASP167 5.0 14.1 1.0

Reference:

C.Tysoe, L.K.Williams, R.Keyzers, N.T.Nguyen, A.Aguda, X.Zhang, C.A.Tarling, R.J.Andersen, G.D.Brayer, S.G.Withers. Structural Templating and Guided Refolding of the Potent Naturally Occurring Peptide Helianthamide Within the Active Site of Amylase, A Diabetes and Obesity Therapeutic Target To Be Published.
Page generated: Sun Jul 14 14:26:30 2024

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