Calcium in PDB 3bsh: Barley Alpha-Amylase Isozyme 1 (AMY1) Double Mutant Y105A/Y380A in Complex with Inhibitor Acarbose

All present enzymatic activity of Barley Alpha-Amylase Isozyme 1 (AMY1) Double Mutant Y105A/Y380A in Complex with Inhibitor Acarbose:
3.2.1.1;

The structure of Barley Alpha-Amylase Isozyme 1 (AMY1) Double Mutant Y105A/Y380A in Complex with Inhibitor Acarbose, PDB code: 3bsh was solved by N.Aghajari, X.Robert, R.Haser, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.19 / 3.00
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	99.500, 72.100, 60.800, 90.00, 90.00, 90.00
R / Rfree (%)	19.7 / 26.8

The binding sites of Calcium atom in the Barley Alpha-Amylase Isozyme 1 (AMY1) Double Mutant Y105A/Y380A in Complex with Inhibitor Acarbose (pdb code 3bsh). 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 Isozyme 1 (AMY1) Double Mutant Y105A/Y380A in Complex with Inhibitor Acarbose, PDB code: 3bsh:
Jump to Calcium binding site number: 1; 2; 3;

Calcium binding site 1 out of 3 in the Barley Alpha-Amylase Isozyme 1 (AMY1) Double Mutant Y105A/Y380A in Complex with Inhibitor 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 Isozyme 1 (AMY1) Double Mutant Y105A/Y380A in Complex with Inhibitor Acarbose within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca500 b:2.8 occ:1.00 OD1 A:ASN92 2.3 7.9 1.0 OD2 A:ASP149 2.3 6.2 1.0 OD1 A:ASP139 2.4 8.2 1.0 O A:ALA142 2.5 4.8 1.0 O A:GLY184 2.8 5.9 1.0 CG A:ASP139 3.2 8.8 1.0 OD2 A:ASP139 3.3 10.2 1.0 CG A:ASP149 3.4 5.8 1.0 CG A:ASN92 3.4 7.8 1.0 C A:ALA142 3.7 5.4 1.0 C A:GLY184 3.7 7.1 1.0 CB A:ASP149 3.8 7.2 1.0 O A:GLY141 3.9 4.5 1.0 O A:ASN92 4.0 8.9 1.0 CA A:GLY184 4.1 7.2 1.0 ND2 A:ASN92 4.1 5.2 1.0 C A:GLY141 4.2 4.6 1.0 CA A:ASP143 4.3 9.2 1.0 OD1 A:ASP149 4.5 5.6 1.0 N A:ASP143 4.5 6.3 1.0 N A:ALA142 4.5 4.2 1.0 CB A:ASN92 4.6 8.3 1.0 CB A:ASP139 4.6 7.3 1.0 N A:GLY141 4.7 4.6 1.0 CA A:GLY141 4.7 4.4 1.0 CA A:ALA142 4.7 4.5 1.0 C A:ASN92 4.8 8.5 1.0 CA A:ASP149 4.9 8.8 1.0 N A:TYR185 4.9 6.1 1.0 CA A:ASN92 5.0 8.3 1.0

Calcium binding site 2 out of 3 in the Barley Alpha-Amylase Isozyme 1 (AMY1) Double Mutant Y105A/Y380A in Complex with Inhibitor 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 Isozyme 1 (AMY1) Double Mutant Y105A/Y380A in Complex with Inhibitor Acarbose within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca501 b:7.6 occ:1.00 O A:ASP114 2.2 14.0 1.0 O A:THR112 2.3 15.5 1.0 OE2 A:GLU109 2.5 5.5 1.0 OD1 A:ASP118 2.5 11.6 1.0 OD2 A:ASP118 2.7 9.8 1.0 CG A:ASP118 3.0 9.8 1.0 OE1 A:GLU109 3.1 5.7 1.0 CD A:GLU109 3.2 6.5 1.0 C A:THR112 3.4 14.8 1.0 C A:ASP114 3.5 14.4 1.0 N A:THR112 3.8 12.2 1.0 C A:SER113 4.0 16.5 1.0 O A:SER113 4.1 16.6 1.0 CA A:GLY115 4.1 13.5 1.0 OG1 A:THR112 4.1 15.0 1.0 CA A:THR112 4.2 13.5 1.0 N A:ASP114 4.2 15.4 1.0 N A:GLY115 4.3 14.6 1.0 N A:GLY111 4.3 9.4 1.0 N A:GLY110 4.3 8.3 1.0 N A:SER113 4.3 16.0 1.0 CA A:ASP114 4.5 14.6 1.0 CB A:ASP118 4.5 9.5 1.0 CA A:SER113 4.5 17.0 1.0 C A:GLY115 4.5 12.7 1.0 CG A:GLU109 4.6 5.8 1.0 O A:ARG116 4.6 11.7 1.0 N A:ARG116 4.7 12.5 1.0 CB A:THR112 4.8 13.0 1.0 C A:GLY111 4.8 11.0 1.0 CA A:GLY110 4.9 8.3 1.0

Calcium binding site 3 out of 3 in the Barley Alpha-Amylase Isozyme 1 (AMY1) Double Mutant Y105A/Y380A in Complex with Inhibitor 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 Isozyme 1 (AMY1) Double Mutant Y105A/Y380A in Complex with Inhibitor Acarbose within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca502 b:3.5 occ:1.00 O A:PHE144 2.3 14.4 1.0 O A:ALA147 2.3 9.9 1.0 OD2 A:ASP128 2.3 12.2 1.0 OD1 A:ASP143 2.4 11.7 1.0 OD1 A:ASP149 2.6 5.6 1.0 CG A:ASP128 3.1 13.5 1.0 CG A:ASP143 3.2 11.4 1.0 OD1 A:ASP128 3.2 13.7 1.0 OD2 A:ASP143 3.2 13.8 1.0 C A:PHE144 3.3 14.6 1.0 C A:ALA147 3.4 10.6 1.0 CG A:ASP149 3.6 5.8 1.0 O A:ALA145 3.7 17.1 1.0 N A:ASP149 3.8 9.9 1.0 N A:PHE144 3.9 11.6 1.0 CB A:ASP149 4.1 7.2 1.0 N A:ALA145 4.1 15.7 1.0 N A:PRO148 4.2 11.1 1.0 CA A:PHE144 4.2 13.2 1.0 CA A:PRO148 4.2 11.5 1.0 C A:PRO148 4.2 11.0 1.0 C A:ALA145 4.2 15.3 1.0 CA A:ALA145 4.3 15.2 1.0 N A:ALA147 4.3 10.5 1.0 CA A:ALA147 4.4 10.2 1.0 CA A:ASP149 4.5 8.8 1.0 CB A:ASP128 4.6 12.1 1.0 CE2 A:TYR131 4.6 15.3 1.0 CB A:ASP143 4.7 10.1 1.0 OD2 A:ASP149 4.7 6.2 1.0 CB A:PHE144 4.7 14.5 1.0 CD2 A:TYR131 4.7 15.7 1.0 C A:ASP143 4.9 10.8 1.0

M.M.Nielsen, E.S.Seo, S.Bozonnet, N.Aghajari, X.Robert, R.Haser, B.Svensson. Multi-Site Substrate Binding and Interplay in Barley Alpha-Amylase 1 Febs Lett. V. 582 2567 2008.
ISSN: ISSN 0014-5793
PubMed: 18588886
DOI: 10.1016/J.FEBSLET.2008.06.027