Calcium in PDB 1pif: Pig Alpha-Amylase

All present enzymatic activity of Pig Alpha-Amylase:
3.2.1.1;

The structure of Pig Alpha-Amylase, PDB code: 1pif was solved by M.Machius, L.Vertesy, R.Huber, G.Wiegand, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	7.00 / 2.30
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	70.700, 114.900, 118.900, 90.00, 90.00, 90.00
R / Rfree (%)	17.1 / 20.8

The structure of Pig Alpha-Amylase also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Calcium atom in the Pig Alpha-Amylase (pdb code 1pif). 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 Pig Alpha-Amylase, PDB code: 1pif:

Calcium binding site 1 out of 1 in the Pig Alpha-Amylase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Pig Alpha-Amylase within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca500 b:26.7 occ:1.00 O A:HOH1084 2.3 24.1 1.0 O A:HIS201 2.4 28.4 1.0 OD2 A:ASP167 2.4 32.4 1.0 O A:HOH1022 2.4 31.5 1.0 OD1 A:ASN100 2.4 37.7 1.0 O A:ARG158 2.5 33.4 1.0 OD1 A:ASP167 2.5 32.1 1.0 CG A:ASP167 2.8 31.3 1.0 CG A:ASN100 3.4 29.8 1.0 C A:ARG158 3.5 30.1 1.0 C A:HIS201 3.6 26.8 1.0 ND2 A:ASN100 3.7 27.4 1.0 CB A:HIS201 4.2 28.0 1.0 CA A:ARG158 4.2 29.7 1.0 CB A:ASP167 4.3 31.8 1.0 O A:ASN100 4.3 29.0 1.0 O A:HOH1038 4.3 36.1 1.0 CA A:HIS201 4.5 29.6 1.0 ND2 A:ASN137 4.5 36.9 1.0 N A:ASP159 4.5 31.8 1.0 N A:MET202 4.5 25.3 1.0 O A:CYS160 4.6 32.2 1.0 CG A:MET202 4.6 25.8 1.0 CA A:MET202 4.7 25.5 1.0 O A:VAL157 4.7 33.9 1.0 CA A:ASP159 4.8 31.7 1.0 CB A:ASN100 4.8 27.3 1.0 O A:LEU168 4.9 35.5 1.0

M.Machius, L.Vertesy, R.Huber, G.Wiegand. Carbohydrate and Protein-Based Inhibitors of Porcine Pancreatic Alpha-Amylase: Structure Analysis and Comparison of Their Binding Characteristics. J.Mol.Biol. V. 260 409 1996.
ISSN: ISSN 0022-2836
PubMed: 8757803
DOI: 10.1006/JMBI.1996.0410