Calcium in PDB 1axk: Engineered Bacillus Bifunctional Enzyme Gluxyn-1

All present enzymatic activity of Engineered Bacillus Bifunctional Enzyme Gluxyn-1:
3.2.1.73; 3.2.1.8;

The structure of Engineered Bacillus Bifunctional Enzyme Gluxyn-1, PDB code: 1axk was solved by J.Ay, U.Heinemann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.96 / 2.10
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	45.270, 133.700, 77.950, 90.00, 99.76, 90.00
R / Rfree (%)	17.6 / 22.4

The binding sites of Calcium atom in the Engineered Bacillus Bifunctional Enzyme Gluxyn-1 (pdb code 1axk). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Engineered Bacillus Bifunctional Enzyme Gluxyn-1, PDB code: 1axk:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Engineered Bacillus Bifunctional Enzyme Gluxyn-1


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Engineered Bacillus Bifunctional Enzyme Gluxyn-1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca395 b:40.3 occ:1.00 O A:GLY384 2.2 33.9 1.0 O A:PRO348 2.5 21.1 1.0 O A:ASP149 2.5 21.3 1.0 OD1 A:ASP149 2.6 24.4 1.0 C A:GLY384 3.4 35.9 1.0 C A:ASP149 3.5 21.1 1.0 C A:PRO348 3.7 22.3 1.0 CG A:ASP149 3.7 26.1 1.0 CA A:ASP149 3.9 21.6 1.0 O A:LYS349 3.9 27.9 1.0 C A:LYS349 4.2 26.5 1.0 CB A:LYS349 4.3 27.3 1.0 CG A:LYS385 4.3 34.0 1.0 N A:LYS385 4.3 33.0 1.0 CA A:LYS385 4.3 29.7 1.0 CB A:ASP149 4.4 24.0 1.0 CA A:GLY384 4.4 38.2 1.0 CA A:PRO348 4.6 23.9 1.0 CA A:LYS349 4.6 25.4 1.0 OD2 A:ASP149 4.6 28.0 1.0 N A:LYS349 4.6 20.3 1.0 N A:TRP150 4.6 19.0 1.0 N A:SER350 4.7 27.1 1.0 O A:ASP383 4.7 43.6 1.0 CA A:SER350 4.9 28.6 1.0 O A:TYR148 5.0 21.7 1.0 CB A:PRO348 5.0 25.1 1.0

Calcium binding site 2 out of 2 in the Engineered Bacillus Bifunctional Enzyme Gluxyn-1


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Engineered Bacillus Bifunctional Enzyme Gluxyn-1 within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca395 b:20.2 occ:1.00 O B:GLY384 2.2 17.2 1.0 OD1 B:ASP149 2.3 12.4 1.0 O B:PRO348 2.3 17.3 1.0 O B:ASP149 2.4 11.6 1.0 O B:HOH492 2.8 29.1 1.0 C B:GLY384 3.4 18.8 1.0 CG B:ASP149 3.4 13.7 1.0 C B:ASP149 3.4 12.5 1.0 C B:PRO348 3.5 16.5 1.0 CA B:ASP149 3.9 11.9 1.0 CA B:GLY384 4.2 16.9 1.0 CB B:ASP149 4.2 12.6 1.0 CA B:PRO348 4.3 17.2 1.0 O B:LYS349 4.3 16.5 1.0 OD2 B:ASP149 4.4 14.4 1.0 CB B:LYS349 4.4 19.9 1.0 O B:HOH472 4.4 30.5 1.0 C B:LYS349 4.4 19.8 1.0 N B:LYS385 4.5 16.8 1.0 N B:LYS349 4.5 15.3 1.0 N B:TRP150 4.6 9.9 1.0 CB B:PRO348 4.6 19.4 1.0 CA B:LYS385 4.7 17.8 1.0 CA B:LYS349 4.7 18.8 1.0 O B:ASP383 4.8 23.5 1.0 CB B:TRP150 4.8 12.1 1.0 CA B:TRP150 4.9 11.7 1.0 CG B:LYS385 5.0 19.9 1.0 N B:SER350 5.0 21.1 1.0

J.Ay, F.Gotz, R.Borriss, U.Heinemann. Structure and Function of the Bacillus Hybrid Enzyme Gluxyn-1: Native-Like Jellyroll Fold Preserved After Insertion of Autonomous Globular Domain. Proc.Natl.Acad.Sci.Usa V. 95 6613 1998.
ISSN: ISSN 0027-8424
PubMed: 9618460
DOI: 10.1073/PNAS.95.12.6613