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Calcium in PDB 1b2y: Structure of Human Pancreatic Alpha-Amylase in Complex with the Carbohydrate Inhibitor Acarbose

Enzymatic activity of Structure of Human Pancreatic Alpha-Amylase in Complex with the Carbohydrate Inhibitor Acarbose

All present enzymatic activity of Structure of Human Pancreatic Alpha-Amylase in Complex with the Carbohydrate Inhibitor Acarbose:
3.2.1.1;

Protein crystallography data

The structure of Structure of Human Pancreatic Alpha-Amylase in Complex with the Carbohydrate Inhibitor Acarbose, PDB code: 1b2y was solved by V.Nahoum, F.Payan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 11.00 / 3.20
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 53.110, 75.100, 137.130, 90.00, 90.00, 90.00
R / Rfree (%) 19.1 / 21.7

Other elements in 1b2y:

The structure of Structure of Human Pancreatic Alpha-Amylase in Complex with the Carbohydrate Inhibitor Acarbose also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the Structure of Human Pancreatic Alpha-Amylase in Complex with the Carbohydrate Inhibitor Acarbose (pdb code 1b2y). 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 Structure of Human Pancreatic Alpha-Amylase in Complex with the Carbohydrate Inhibitor Acarbose, PDB code: 1b2y:

Calcium binding site 1 out of 1 in 1b2y

Go back to Calcium Binding Sites List in 1b2y
Calcium binding site 1 out of 1 in the Structure of Human Pancreatic Alpha-Amylase in Complex with the Carbohydrate Inhibitor Acarbose


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of Human Pancreatic Alpha-Amylase in Complex with the Carbohydrate Inhibitor Acarbose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca500

b:30.0
occ:1.00
 OD1 A:ASN100 2.4 17.1 1.0
O A:ARG158 2.5 10.2 1.0
OD2 A:ASP167 2.5 26.3 1.0
O A:HOH520 2.6 24.6 1.0
O A:HIS201 2.6 13.9 1.0
OD1 A:ASP167 2.6 27.0 1.0
O A:HOH729 2.7 8.4 1.0
CG A:ASP167 2.9 30.6 1.0
O A:HOH527 3.0 17.6 1.0
CG A:ASN100 3.5 20.4 1.0
C A:ARG158 3.6 16.9 1.0
C A:HIS201 3.8 2.0 1.0
ND2 A:ASN100 3.9 18.2 1.0
CA A:ARG158 4.2 16.4 1.0
O A:ASN100 4.3 17.6 1.0
CB A:ASP167 4.4 28.1 1.0
ND2 A:ASN137 4.4 9.0 1.0
CB A:HIS201 4.5 16.1 1.0
CA A:MET202 4.6 2.0 1.0
N A:MET202 4.6 2.0 1.0
N A:ASP159 4.6 4.2 1.0
O A:LEU168 4.6 10.2 1.0
CA A:HIS201 4.7 2.0 1.0
CG A:MET202 4.7 16.1 1.0
CB A:ASN100 4.7 16.0 1.0
CA A:ASP159 4.9 5.7 1.0
O A:VAL157 4.9 24.9 1.0
O A:CYS160 4.9 28.1 1.0
CB A:ARG158 4.9 8.1 1.0

Reference:

V.Nahoum, G.Roux, V.Anton, P.Rouge, A.Puigserver, H.Bischoff, B.Henrissat, F.Payan. Crystal Structures of Human Pancreatic Alpha-Amylase in Complex with Carbohydrate and Proteinaceous Inhibitors. Biochem.J. V.Pt 1 201 2000.
ISSN: ISSN 0264-6021
PubMed: 10657258
DOI: 10.1042/0264-6021:3460201
Page generated: Sat Dec 12 02:49:15 2020

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