Calcium in PDB 1jdd: Mutant (E219Q) Maltotetraose-Forming Exo-Amylase Cocrystallized with Maltotetraose (Crystal Type 2)

All present enzymatic activity of Mutant (E219Q) Maltotetraose-Forming Exo-Amylase Cocrystallized with Maltotetraose (Crystal Type 2):
3.2.1.60;

The structure of Mutant (E219Q) Maltotetraose-Forming Exo-Amylase Cocrystallized with Maltotetraose (Crystal Type 2), PDB code: 1jdd 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 / 1.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	65.600, 170.700, 46.800, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Calcium atom in the Mutant (E219Q) Maltotetraose-Forming Exo-Amylase Cocrystallized with Maltotetraose (Crystal Type 2) (pdb code 1jdd). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Mutant (E219Q) Maltotetraose-Forming Exo-Amylase Cocrystallized with Maltotetraose (Crystal Type 2), PDB code: 1jdd:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Mutant (E219Q) Maltotetraose-Forming Exo-Amylase Cocrystallized with Maltotetraose (Crystal Type 2)


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Mutant (E219Q) Maltotetraose-Forming Exo-Amylase Cocrystallized with Maltotetraose (Crystal Type 2) within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca451 b:21.2 occ:1.00 OD2 A:ASP162 2.3 14.7 1.0 O A:GLY197 2.3 15.7 1.0 O A:ASP154 2.4 18.6 1.0 OD2 A:ASP151 2.5 17.3 1.0 O A:HOH594 2.5 15.0 1.0 OD1 A:ASN116 2.6 13.2 1.0 OD1 A:ASP151 2.7 18.4 1.0 CG A:ASP151 2.9 18.1 1.0 C A:GLY197 3.4 15.8 1.0 CG A:ASP162 3.4 15.0 1.0 CG A:ASN116 3.5 12.5 1.0 C A:ASP154 3.6 17.8 1.0 CA A:GLY197 3.7 15.5 1.0 ND2 A:ASN116 3.9 12.1 1.0 CB A:ASP162 4.0 16.4 1.0 CA A:ARG155 4.2 18.0 1.0 C A:GLY153 4.2 18.7 1.0 O A:GLY153 4.2 18.7 1.0 N A:ARG155 4.3 17.5 1.0 CB A:ASP151 4.4 18.6 1.0 N A:ASP154 4.4 18.3 1.0 O A:HOH515 4.4 17.2 1.0 O A:ASN116 4.4 16.9 1.0 OD1 A:ASP162 4.5 15.5 1.0 NH1 A:ARG137 4.5 18.7 1.0 N A:TYR198 4.6 15.8 1.0 CA A:GLY153 4.6 18.6 1.0 CA A:ASP154 4.7 18.1 1.0 O A:LEU163 4.7 18.8 1.0 N A:GLY153 4.8 18.7 1.0 CB A:ASN116 4.8 14.2 1.0

Calcium binding site 2 out of 2 in the Mutant (E219Q) Maltotetraose-Forming Exo-Amylase Cocrystallized with Maltotetraose (Crystal Type 2)


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Mutant (E219Q) Maltotetraose-Forming Exo-Amylase Cocrystallized with Maltotetraose (Crystal Type 2) within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca452 b:43.1 occ:1.00 OD1 A:ASP1 1.9 52.9 1.0 OE2 A:GLU17 2.2 21.1 1.0 O A:GLN2 2.4 48.0 1.0 O A:HIS13 2.5 19.2 1.0 OD1 A:ASP16 2.6 27.8 1.0 ND1 A:HIS13 2.7 22.4 1.0 CG A:ASP1 3.0 53.3 1.0 CD A:GLU17 3.1 18.6 1.0 OD2 A:ASP1 3.5 53.4 1.0 CE1 A:HIS13 3.6 23.5 1.0 C A:HIS13 3.6 18.8 1.0 CG A:ASP16 3.7 27.0 1.0 C A:GLN2 3.7 48.2 1.0 CG A:HIS13 3.7 21.6 1.0 CG A:GLU17 3.8 16.4 1.0 OD2 A:ASP16 4.1 29.7 1.0 CB A:HIS13 4.1 20.2 1.0 OE1 A:GLU17 4.2 19.4 1.0 N A:GLN2 4.2 51.6 1.0 CA A:GLY14 4.3 18.8 1.0 C A:ASP1 4.3 52.5 1.0 CB A:ASP1 4.3 53.5 1.0 CE A:LYS108 4.4 26.4 1.0 N A:GLY14 4.4 18.6 1.0 CA A:HIS13 4.5 19.0 1.0 CA A:GLN2 4.5 50.2 1.0 CA A:ALA3 4.5 43.1 1.0 CA A:ASP1 4.6 53.1 1.0 N A:ASP16 4.6 19.8 1.0 NZ A:LYS108 4.6 26.7 1.0 N A:GLU17 4.6 18.0 1.0 N A:ALA3 4.6 45.8 1.0 O A:ASP1 4.7 52.8 1.0 C A:ASP16 4.7 19.4 1.0 NE2 A:HIS13 4.7 23.7 1.0 C A:GLY14 4.8 19.0 1.0 CB A:GLN2 4.8 52.9 1.0 N A:GLY15 4.8 19.1 1.0 CD2 A:HIS13 4.8 22.5 1.0 CB A:ALA3 4.9 43.1 1.0 CB A:ASP16 4.9 23.5 1.0 CA A:ASP16 4.9 20.0 1.0 CB A:GLU17 5.0 14.9 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