Calcium in PDB 3kwx: Chemically Modified Taka Alpha-Amylase

All present enzymatic activity of Chemically Modified Taka Alpha-Amylase:
3.2.1.1;

The structure of Chemically Modified Taka Alpha-Amylase, PDB code: 3kwx was solved by K.S.Siddiqui, S.J.Harrop, A.Poljak, D.De Francisci, G.Guerriero, O.Pilak, D.Burg, M.J.Raftery, D.M.Parkin, J.Trewhella, R.Cavicchioli, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.18 / 2.40
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	120.727, 120.727, 115.676, 90.00, 90.00, 120.00
R / Rfree (%)	17.5 / 21

The binding sites of Calcium atom in the Chemically Modified Taka Alpha-Amylase (pdb code 3kwx). 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 Chemically Modified Taka Alpha-Amylase, PDB code: 3kwx:

Calcium binding site 1 out of 1 in the Chemically Modified Taka Alpha-Amylase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Chemically Modified Taka Alpha-Amylase within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca480 b:37.3 occ:1.00 O A:HIS210 2.5 35.4 1.0 OD2 A:ASP175 2.5 36.9 1.0 OD1 A:ASN121 2.5 33.8 1.0 O A:HOH607 2.5 35.1 1.0 O A:GLU162 2.5 39.5 1.0 O A:HOH605 2.6 35.1 1.0 O A:HOH606 2.6 40.0 1.0 OD1 A:ASP175 2.7 36.9 1.0 CG A:ASP175 2.9 33.9 1.0 C A:GLU162 3.6 42.6 1.0 C A:HIS210 3.6 36.0 1.0 CG A:ASN121 3.6 34.3 1.0 CA A:GLU162 4.1 41.4 1.0 ND2 A:ASN121 4.2 31.9 1.0 CB A:HIS210 4.3 32.5 1.0 ND1 A:HIS147 4.4 43.0 1.0 O A:LEU176 4.4 36.1 1.0 O A:ASN121 4.4 33.9 1.0 CB A:ASP175 4.4 33.3 1.0 CG2 A:VAL211 4.5 37.1 1.0 CA A:HIS210 4.5 35.0 1.0 CE1 A:HIS147 4.5 44.9 1.0 N A:VAL211 4.5 38.1 1.0 O A:CYS164 4.5 39.5 1.0 CA A:VAL211 4.6 39.0 1.0 N A:ASP163 4.6 39.5 1.0 O A:VAL161 4.7 39.8 1.0 CB A:ASN121 4.8 33.0 1.0 CB A:GLU162 4.9 43.3 1.0 CA A:ASP163 4.9 42.1 1.0

K.S.Siddiqui, A.Poljak, D.De Francisci, G.Guerriero, O.Pilak, D.Burg, M.J.Raftery, D.M.Parkin, J.Trewhella, R.Cavicchioli. A Modified Alpha-Amylase with A Molten-Globule State Has Enhanced Thermal Stability To Be Published.