Calcium in PDB 6jqb: The Structure of Maltooligosaccharide-Forming Amylase From Pseudomonas Saccharophila STB07 with Pseudo-Maltoheptaose

All present enzymatic activity of The Structure of Maltooligosaccharide-Forming Amylase From Pseudomonas Saccharophila STB07 with Pseudo-Maltoheptaose:
3.2.1.60;

The structure of The Structure of Maltooligosaccharide-Forming Amylase From Pseudomonas Saccharophila STB07 with Pseudo-Maltoheptaose, PDB code: 6jqb was solved by Z.F.Li, X.F.Ban, Z.Q.Zhang, C.M.Li, Z.B.Gu, T.C.Jin, Y.L.Li, Y.H.Shang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.29 / 1.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	47.900, 63.735, 163.727, 90.00, 90.00, 90.00
R / Rfree (%)	17 / 18.6

The binding sites of Calcium atom in the The Structure of Maltooligosaccharide-Forming Amylase From Pseudomonas Saccharophila STB07 with Pseudo-Maltoheptaose (pdb code 6jqb). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the The Structure of Maltooligosaccharide-Forming Amylase From Pseudomonas Saccharophila STB07 with Pseudo-Maltoheptaose, PDB code: 6jqb:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the The Structure of Maltooligosaccharide-Forming Amylase From Pseudomonas Saccharophila STB07 with Pseudo-Maltoheptaose


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of The Structure of Maltooligosaccharide-Forming Amylase From Pseudomonas Saccharophila STB07 with Pseudo-Maltoheptaose within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca604 b:9.6 occ:0.00 O A:GLY197 2.4 9.9 1.0 OD2 A:ASP151 2.4 10.5 1.0 O A:HOH738 2.4 9.3 1.0 O A:ASP154 2.5 10.2 1.0 OD1 A:ASN116 2.5 9.3 1.0 OD1 A:ASP151 2.6 9.8 1.0 OD2 A:ASP162 2.6 12.5 1.0 CG A:ASP151 2.8 9.1 1.0 C A:GLY197 3.4 9.1 1.0 HA A:ARG155 3.4 13.6 1.0 HB3 A:ASP162 3.5 12.2 1.0 CG A:ASN116 3.5 9.1 1.0 HA2 A:GLY197 3.5 11.2 1.0 HA3 A:GLY197 3.6 11.2 1.0 C A:ASP154 3.6 9.8 1.0 HD21 A:ASN116 3.7 11.3 1.0 CG A:ASP162 3.7 10.5 1.0 CA A:GLY197 3.7 9.3 1.0 HH11 A:ARG137 4.0 15.2 1.0 ND2 A:ASN116 4.0 9.4 1.0 H A:GLY153 4.1 13.9 1.0 CB A:ASP162 4.1 10.1 1.0 C A:GLY153 4.2 9.9 1.0 O A:GLY153 4.2 10.8 1.0 HD2 A:ARG137 4.2 14.9 1.0 CA A:ARG155 4.3 11.3 1.0 CB A:ASP151 4.3 10.8 1.0 HE2 A:PHE194 4.3 13.8 1.0 HA3 A:GLY153 4.4 12.8 1.0 N A:ASP154 4.4 10.7 1.0 N A:ARG155 4.4 10.7 1.0 O A:HOH752 4.4 11.0 1.0 O A:ASN116 4.4 9.1 1.0 HB3 A:TYR198 4.5 11.7 1.0 HD1 A:TYR198 4.5 11.1 1.0 HA A:ASN116 4.5 9.6 1.0 N A:TYR198 4.6 9.4 1.0 HB2 A:ASP151 4.6 12.9 1.0 CA A:GLY153 4.7 10.6 1.0 CA A:ASP154 4.7 10.4 1.0 HB2 A:ASP162 4.7 12.2 1.0 NH1 A:ARG137 4.7 12.7 1.0 HB3 A:ASP151 4.7 12.9 1.0 O A:LEU163 4.7 11.0 1.0 H A:ASP154 4.7 12.8 1.0 N A:GLY153 4.7 11.6 1.0 CB A:ASN116 4.8 8.7 1.0 HA A:TYR198 4.8 12.0 1.0 OD1 A:ASP162 4.8 10.9 1.0 HD22 A:ASN116 4.8 11.3 1.0 HH12 A:ARG137 4.9 15.2 1.0 HB2 A:ARG137 4.9 14.0 1.0 HB3 A:ARG155 4.9 14.9 1.0 H A:PHE156 5.0 13.4 1.0 HB2 A:ASN116 5.0 10.5 1.0

Calcium binding site 2 out of 2 in the The Structure of Maltooligosaccharide-Forming Amylase From Pseudomonas Saccharophila STB07 with Pseudo-Maltoheptaose


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of The Structure of Maltooligosaccharide-Forming Amylase From Pseudomonas Saccharophila STB07 with Pseudo-Maltoheptaose within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca605 b:15.3 occ:0.00 O A:GLN2 2.3 13.4 1.0 OE1 A:GLU17 2.3 13.4 1.0 OD1 A:ASP1 2.3 30.7 1.0 O A:HIS13 2.4 11.0 1.0 OD1 A:ASP16 2.4 11.9 1.0 ND1 A:HIS13 2.5 11.8 1.0 OD2 A:ASP1 2.7 30.4 1.0 CG A:ASP1 2.8 28.9 1.0 CE1 A:HIS13 3.3 13.1 1.0 HE1 A:HIS13 3.4 15.8 1.0 C A:GLN2 3.4 15.3 1.0 C A:HIS13 3.4 10.6 1.0 CG A:ASP16 3.5 13.0 1.0 HB3 A:HIS13 3.5 12.9 1.0 CD A:GLU17 3.5 11.3 1.0 H A:GLN2 3.5 23.1 1.0 CG A:HIS13 3.6 11.5 1.0 HZ1 A:LYS108 3.6 23.0 1.0 HA A:ALA3 3.7 16.6 1.0 HA3 A:GLY14 3.8 13.1 1.0 HG2 A:GLU17 3.8 12.8 1.0 N A:GLN2 3.8 19.2 1.0 OD2 A:ASP16 3.8 14.3 1.0 CB A:HIS13 3.9 10.8 1.0 H A:ASP16 4.0 11.8 1.0 HZ3 A:LYS108 4.2 23.0 1.0 HE2 A:LYS108 4.2 22.1 1.0 CA A:GLN2 4.2 18.9 1.0 CG A:GLU17 4.2 10.6 1.0 CB A:ASP1 4.2 26.9 1.0 NZ A:LYS108 4.3 19.2 1.0 CA A:HIS13 4.3 10.5 1.0 N A:ALA3 4.3 14.7 1.0 N A:GLY14 4.3 10.8 1.0 O A:HOH706 4.3 22.7 1.0 C A:ASP1 4.4 21.2 1.0 OE2 A:GLU17 4.4 11.4 1.0 CA A:ALA3 4.4 13.8 1.0 CA A:GLY14 4.5 10.9 1.0 NE2 A:HIS13 4.5 13.2 1.0 HA A:ASP1 4.6 29.4 1.0 HB3 A:GLN2 4.7 26.3 1.0 CD2 A:HIS13 4.7 12.9 1.0 HA A:HIS13 4.7 12.6 1.0 HB2 A:ASP1 4.7 32.2 1.0 CA A:ASP1 4.7 24.4 1.0 HB3 A:ASP1 4.8 32.2 1.0 HG3 A:GLU17 4.8 12.8 1.0 CE A:LYS108 4.8 18.4 1.0 N A:ASP16 4.8 9.8 1.0 CB A:ASP16 4.8 10.9 1.0 N A:GLU17 4.8 8.5 1.0 C A:ASP16 4.8 9.4 1.0 HB2 A:HIS13 4.8 12.9 1.0 HA A:GLU17 4.9 10.5 1.0 H A:GLU17 4.9 10.2 1.0 HA A:GLN2 4.9 22.7 1.0 H A:GLY15 5.0 13.1 1.0 HZ2 A:LYS108 5.0 23.0 1.0 C A:GLY14 5.0 10.8 1.0

Z.Zhang, T.Jin, X.Xie, X.Ban, C.Li, Y.Hong, L.Cheng, Z.Gu, Z.Li. Structure of Maltotetraose-Forming Amylase From Pseudomonas Saccharophila STB07 Provides Insights Into Its Product Specificity. Int.J.Biol.Macromol. 2019.
ISSN: ISSN 0141-8130
PubMed: 31751711
DOI: 10.1016/J.IJBIOMAC.2019.11.006