Calcium in PDB 1jda: Maltotetraose-Forming Exo-Amylase

All present enzymatic activity of Maltotetraose-Forming Exo-Amylase:
3.2.1.60;

The structure of Maltotetraose-Forming Exo-Amylase, PDB code: 1jda was solved by Y.Yoshioka, K.Hasegawa, Y.Matsuura, Y.Katsube, M.Kubota, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 2.20
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	65.700, 171.000, 46.800, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Calcium atom in the Maltotetraose-Forming Exo-Amylase (pdb code 1jda). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Maltotetraose-Forming Exo-Amylase, PDB code: 1jda:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Maltotetraose-Forming Exo-Amylase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Maltotetraose-Forming Exo-Amylase within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca454 b:17.7 occ:1.00 O A:HOH502 2.3 19.6 1.0 O A:ASP154 2.4 20.3 1.0 O A:GLY197 2.4 8.4 1.0 OD2 A:ASP151 2.5 20.7 1.0 OD2 A:ASP162 2.5 19.2 1.0 OD1 A:ASN116 2.5 19.0 1.0 OD1 A:ASP151 2.6 16.1 1.0 CG A:ASP151 2.8 20.7 1.0 CG A:ASN116 3.4 18.6 1.0 C A:GLY197 3.5 10.9 1.0 C A:ASP154 3.6 20.2 1.0 CG A:ASP162 3.6 20.6 1.0 CA A:GLY197 3.7 10.8 1.0 ND2 A:ASN116 3.9 16.2 1.0 O A:GLY153 4.1 20.1 1.0 CB A:ASP162 4.1 20.0 1.0 C A:GLY153 4.1 20.4 1.0 O A:HOH574 4.2 23.2 1.0 CA A:ARG155 4.3 21.9 1.0 CB A:ASP151 4.3 20.6 1.0 N A:ARG155 4.3 20.7 1.0 N A:ASP154 4.4 20.1 1.0 O A:ASN116 4.4 16.3 1.0 CA A:GLY153 4.6 20.7 1.0 NH1 A:ARG137 4.6 25.2 1.0 OD1 A:ASP162 4.7 19.5 1.0 CA A:ASP154 4.7 19.7 1.0 N A:TYR198 4.7 9.7 1.0 CB A:ASN116 4.7 18.7 1.0 O A:LEU163 4.7 22.4 1.0 N A:GLY153 4.8 21.2 1.0

Calcium binding site 2 out of 2 in the Maltotetraose-Forming Exo-Amylase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Maltotetraose-Forming Exo-Amylase within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca455 b:58.5 occ:1.00 O A:GLN2 2.4 58.4 1.0 OE2 A:GLU17 2.6 18.4 1.0 O A:HIS13 2.7 15.8 1.0 OD1 A:ASP16 2.7 28.1 1.0 OD1 A:ASP1 2.7 61.7 1.0 ND1 A:HIS13 3.0 26.0 1.0 C A:GLN2 3.5 57.8 1.0 CG A:ASP1 3.5 61.6 1.0 CD A:GLU17 3.6 17.7 1.0 N A:GLN2 3.7 61.0 1.0 CE1 A:HIS13 3.7 25.2 1.0 C A:HIS13 3.8 16.9 1.0 C A:ASP1 3.8 61.7 1.0 CG A:ASP16 3.9 28.1 1.0 CA A:ASP1 3.9 61.8 1.0 CG A:HIS13 4.1 24.8 1.0 OD2 A:ASP1 4.1 60.8 1.0 CG A:GLU17 4.2 16.4 1.0 CA A:ALA3 4.3 51.5 1.0 N A:ALA3 4.3 54.7 1.0 CA A:GLN2 4.3 59.7 1.0 CA A:GLY14 4.3 18.1 1.0 CB A:ASP1 4.3 61.8 1.0 OD2 A:ASP16 4.4 31.6 1.0 CB A:HIS13 4.4 20.3 1.0 CE A:LYS108 4.5 20.6 1.0 N A:GLY14 4.5 17.9 1.0 O A:ASP1 4.5 61.8 1.0 CB A:ALA3 4.6 52.2 1.0 OE1 A:GLU17 4.6 17.8 1.0 N A:ASP16 4.7 19.2 1.0 CA A:HIS13 4.7 18.4 1.0 C A:ASP16 4.7 18.1 1.0 NZ A:LYS108 4.9 20.2 1.0 NE2 A:HIS13 4.9 27.3 1.0 N A:GLU17 4.9 16.8 1.0 C A:GLY14 4.9 18.8 1.0 N A:GLY15 5.0 18.9 1.0 O A:ASP16 5.0 17.9 1.0

Y.Yoshioka, K.Hasegawa, Y.Matsuura, Y.Katsube, M.Kubota. Crystal Structures of A Mutant Maltotetraose-Forming Exo-Amylase Cocrystallized with Maltopentaose. J.Mol.Biol. V. 271 619 1997.
ISSN: ISSN 0022-2836
PubMed: 9281429
DOI: 10.1006/JMBI.1997.1222