Calcium in PDB 1qi3: Mutant (D193N) Maltotetraose-Forming Exo-Amylase in Complex with Maltotetraose

All present enzymatic activity of Mutant (D193N) Maltotetraose-Forming Exo-Amylase in Complex with Maltotetraose:
3.2.1.60;

The structure of Mutant (D193N) Maltotetraose-Forming Exo-Amylase in Complex with Maltotetraose, PDB code: 1qi3 was solved by K.Hasegawa, M.Kubota, Y.Matsuura, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	65.770, 170.800, 46.780, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Calcium atom in the Mutant (D193N) Maltotetraose-Forming Exo-Amylase in Complex with Maltotetraose (pdb code 1qi3). 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 (D193N) Maltotetraose-Forming Exo-Amylase in Complex with Maltotetraose, PDB code: 1qi3:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Mutant (D193N) Maltotetraose-Forming Exo-Amylase in Complex with Maltotetraose


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Mutant (D193N) Maltotetraose-Forming Exo-Amylase in Complex with Maltotetraose within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca451 b:18.4 occ:1.00 OD2 A:ASP162 2.2 14.7 1.0 O A:GLY197 2.4 14.2 1.0 O A:ASP154 2.4 16.6 1.0 O A:HOH553 2.5 16.8 1.0 OD2 A:ASP151 2.5 17.8 1.0 OD1 A:ASN116 2.6 15.8 1.0 OD1 A:ASP151 2.6 18.8 1.0 CG A:ASP151 2.9 18.8 1.0 CG A:ASP162 3.4 15.1 1.0 C A:GLY197 3.4 14.3 1.0 CG A:ASN116 3.6 14.6 1.0 C A:ASP154 3.6 16.9 1.0 CA A:GLY197 3.7 14.2 1.0 ND2 A:ASN116 4.0 13.1 1.0 CB A:ASP162 4.1 16.2 1.0 C A:GLY153 4.2 17.4 1.0 O A:GLY153 4.2 17.2 1.0 CA A:ARG155 4.2 17.7 1.0 CB A:ASP151 4.4 19.0 1.0 N A:ARG155 4.4 16.5 1.0 N A:ASP154 4.4 17.1 1.0 OD1 A:ASP162 4.4 15.3 1.0 NH1 A:ARG137 4.4 18.6 1.0 O A:HOH525 4.5 17.7 1.0 O A:ASN116 4.5 15.0 1.0 N A:TYR198 4.6 14.3 1.0 CA A:GLY153 4.7 17.5 1.0 CA A:ASP154 4.7 16.8 1.0 O A:LEU163 4.7 18.4 1.0 N A:GLY153 4.8 18.0 1.0 CB A:ASN116 4.8 15.2 1.0

Calcium binding site 2 out of 2 in the Mutant (D193N) Maltotetraose-Forming Exo-Amylase in Complex with Maltotetraose


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Mutant (D193N) Maltotetraose-Forming Exo-Amylase in Complex with Maltotetraose within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca452 b:20.1 occ:1.00 OD1 A:ASP1 1.9 50.7 1.0 OE2 A:GLU17 2.0 15.3 1.0 O A:HIS13 2.2 18.3 1.0 OD1 A:ASP16 2.3 21.9 1.0 ND1 A:HIS13 2.4 22.3 1.0 O A:GLN2 2.4 45.4 1.0 CG A:ASP1 3.0 51.0 1.0 CD A:GLU17 3.1 14.5 1.0 CE1 A:HIS13 3.2 22.5 1.0 C A:HIS13 3.3 17.8 1.0 CG A:ASP16 3.4 22.1 1.0 CG A:HIS13 3.4 21.8 1.0 OD2 A:ASP1 3.5 51.9 1.0 C A:GLN2 3.7 45.7 1.0 OD2 A:ASP16 3.7 24.6 1.0 CB A:HIS13 3.8 19.6 1.0 CG A:GLU17 3.8 13.1 1.0 OE1 A:GLU17 4.1 14.6 1.0 N A:GLY14 4.2 17.5 1.0 N A:GLN2 4.2 48.9 1.0 CA A:HIS13 4.2 18.2 1.0 CA A:GLY14 4.2 17.5 1.0 NZ A:LYS108 4.3 23.7 1.0 CB A:ASP1 4.3 50.8 1.0 C A:ASP1 4.4 49.8 1.0 CE A:LYS108 4.4 23.2 1.0 NE2 A:HIS13 4.4 22.9 1.0 O A:HOH775 4.4 43.4 1.0 CD2 A:HIS13 4.5 22.6 1.0 CA A:ALA3 4.5 40.9 1.0 N A:ASP16 4.6 17.7 1.0 CA A:GLN2 4.6 47.6 1.0 N A:ALA3 4.6 43.5 1.0 CA A:ASP1 4.6 50.2 1.0 N A:GLU17 4.7 15.6 1.0 CB A:ASP16 4.7 19.0 1.0 C A:ASP16 4.7 16.7 1.0 O A:ASP1 4.8 50.2 1.0 C A:GLY14 4.8 18.0 1.0 N A:GLY15 4.9 17.6 1.0 CA A:ASP16 4.9 17.3 1.0 CB A:GLN2 5.0 50.4 1.0 O A:TYR12 5.0 17.6 1.0

K.Hasegawa, M.Kubota, Y.Matsuura. Roles of Catalytic Residues in Alpha-Amylases As Evidenced By the Structures of the Product-Complexed Mutants of A Maltotetraose-Forming Amylase. Protein Eng. V. 12 819 1999.
ISSN: ISSN 0269-2139
PubMed: 10556241
DOI: 10.1093/PROTEIN/12.10.819