Calcium in PDB 1bg9: Barley Alpha-Amylase with Substrate Analogue Acarbose

All present enzymatic activity of Barley Alpha-Amylase with Substrate Analogue Acarbose:
3.2.1.1;

The structure of Barley Alpha-Amylase with Substrate Analogue Acarbose, PDB code: 1bg9 was solved by A.Kadziola, R.Haser, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 2.80
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	135.200, 135.200, 79.600, 90.00, 90.00, 120.00
R / Rfree (%)	15.1 / 24.9

The binding sites of Calcium atom in the Barley Alpha-Amylase with Substrate Analogue Acarbose (pdb code 1bg9). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 3 binding sites of Calcium where determined in the Barley Alpha-Amylase with Substrate Analogue Acarbose, PDB code: 1bg9:
Jump to Calcium binding site number: 1; 2; 3;

Calcium binding site 1 out of 3 in the Barley Alpha-Amylase with Substrate Analogue Acarbose


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Barley Alpha-Amylase with Substrate Analogue Acarbose within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca500 b:5.3 occ:1.00 O A:HOH630 2.1 15.8 1.0 O A:ALA141 2.1 7.1 1.0 OD1 A:ASN91 2.2 9.9 1.0 O A:GLY183 2.2 6.8 1.0 OD1 A:ASP138 2.4 7.0 1.0 OD2 A:ASP148 2.5 2.0 1.0 OD2 A:ASP138 2.6 26.3 1.0 CG A:ASP138 2.8 20.2 1.0 C A:GLY183 3.2 8.7 1.0 CG A:ASN91 3.3 5.3 1.0 C A:ALA141 3.3 8.4 1.0 CG A:ASP148 3.6 11.8 1.0 CA A:GLY183 3.7 11.3 1.0 ND2 A:ASN91 3.8 3.6 1.0 O A:GLY140 4.0 14.6 1.0 CB A:ASP148 4.0 6.2 1.0 C A:GLY140 4.1 13.0 1.0 N A:ASP142 4.2 10.1 1.0 O A:ASN91 4.2 9.4 1.0 N A:ALA141 4.3 14.9 1.0 CA A:ASP142 4.3 7.7 1.0 CB A:ASP138 4.4 18.1 1.0 CA A:ALA141 4.4 9.7 1.0 N A:TYR184 4.4 8.3 1.0 CB A:ASN91 4.6 4.1 1.0 OD1 A:ASP148 4.6 8.0 1.0 N A:GLY140 4.7 17.5 1.0 CA A:GLY140 4.8 11.2 1.0 CA A:TYR184 4.9 8.9 1.0 C A:ASN91 5.0 6.1 1.0

Calcium binding site 2 out of 3 in the Barley Alpha-Amylase with Substrate Analogue Acarbose


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Barley Alpha-Amylase with Substrate Analogue Acarbose within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca501 b:15.4 occ:1.00 O A:HOH656 2.1 26.4 1.0 O A:HOH604 2.1 5.0 1.0 O A:ASP113 2.2 12.3 1.0 O A:THR111 2.3 11.2 1.0 OD2 A:ASP117 2.3 14.6 1.0 OD1 A:ASP117 2.5 14.8 1.0 OE2 A:GLU108 2.5 4.1 1.0 CG A:ASP117 2.8 13.3 1.0 OE1 A:GLU108 2.8 8.8 1.0 CD A:GLU108 3.0 10.1 1.0 C A:ASP113 3.4 9.3 1.0 C A:THR111 3.6 9.7 1.0 N A:THR111 4.1 12.6 1.0 OG1 A:THR111 4.2 2.0 1.0 N A:ASP113 4.2 12.0 1.0 C A:PRO112 4.2 11.3 1.0 CB A:ASP117 4.3 11.2 1.0 N A:ALA114 4.3 12.1 1.0 CA A:ALA114 4.3 9.5 1.0 O A:PRO112 4.4 18.9 1.0 CA A:THR111 4.4 8.6 1.0 O A:HOH687 4.4 59.8 1.0 O A:ARG115 4.5 8.2 1.0 CA A:ASP113 4.5 8.2 1.0 N A:PRO112 4.5 10.3 1.0 N A:GLY109 4.5 9.9 1.0 CG A:GLU108 4.5 3.2 1.0 CA A:PRO112 4.6 8.7 1.0 N A:GLY110 4.7 6.6 1.0 C A:ALA114 4.7 11.2 1.0 O A:HOH724 4.8 51.2 1.0

Calcium binding site 3 out of 3 in the Barley Alpha-Amylase with Substrate Analogue Acarbose


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of Barley Alpha-Amylase with Substrate Analogue Acarbose within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca502 b:17.5 occ:1.00 O A:ALA146 2.1 14.8 1.0 O A:PHE143 2.1 15.6 1.0 OD1 A:ASP148 2.4 8.0 1.0 OD2 A:ASP127 2.4 21.8 1.0 OD1 A:ASP127 2.6 24.0 1.0 OD1 A:ASP142 2.6 26.0 1.0 CG A:ASP127 2.8 15.8 1.0 CG A:ASP142 3.3 22.1 1.0 C A:PHE143 3.4 11.7 1.0 C A:ALA146 3.4 8.8 1.0 OD2 A:ASP142 3.5 24.6 1.0 O A:GLY144 3.5 24.3 1.0 CG A:ASP148 3.5 11.8 1.0 N A:ASP148 4.0 10.7 1.0 N A:PHE143 4.0 9.1 1.0 C A:PRO147 4.2 11.0 1.0 C A:GLY144 4.2 12.8 1.0 N A:ALA146 4.2 8.0 1.0 N A:PRO147 4.2 6.8 1.0 N A:GLY144 4.2 10.6 1.0 CB A:ASP148 4.2 6.2 1.0 CB A:ASP127 4.3 9.6 1.0 CA A:PHE143 4.3 10.5 1.0 CA A:GLY144 4.4 9.2 1.0 CA A:ALA146 4.4 7.2 1.0 CA A:PRO147 4.4 8.2 1.0 OD2 A:ASP148 4.5 2.0 1.0 CA A:ASP148 4.6 9.0 1.0 CB A:ASP142 4.7 11.2 1.0 CB A:PHE143 4.7 3.4 1.0 O A:PRO147 4.7 10.9 1.0 CA A:ASP142 5.0 7.7 1.0 C A:ASP142 5.0 9.6 1.0 CD2 A:TYR130 5.0 7.6 1.0

A.Kadziola, M.Sogaard, B.Svensson, R.Haser. Molecular Structure of A Barley Alpha-Amylase-Inhibitor Complex: Implications For Starch Binding and Catalysis. J.Mol.Biol. V. 278 205 1998.
ISSN: ISSN 0022-2836
PubMed: 9571044
DOI: 10.1006/JMBI.1998.1683