Calcium in PDB 2y6g: Cellopentaose Binding Mutated (X-2 L110F) CBM4-2 Carbohydrate Binding Module From A Thermostable Rhodothermus Marinus Xylanase

All present enzymatic activity of Cellopentaose Binding Mutated (X-2 L110F) CBM4-2 Carbohydrate Binding Module From A Thermostable Rhodothermus Marinus Xylanase:
3.2.1.8;

The structure of Cellopentaose Binding Mutated (X-2 L110F) CBM4-2 Carbohydrate Binding Module From A Thermostable Rhodothermus Marinus Xylanase, PDB code: 2y6g was solved by L.Von Schantz, M.Hakansson, D.T.Logan, B.Walse, J.Osterlin, E.Nordberg-Karlsson, M.Ohlin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.30
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	48.560, 49.720, 62.520, 90.00, 90.00, 90.00
R / Rfree (%)	13.2 / 18.3

The binding sites of Calcium atom in the Cellopentaose Binding Mutated (X-2 L110F) CBM4-2 Carbohydrate Binding Module From A Thermostable Rhodothermus Marinus Xylanase (pdb code 2y6g). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Cellopentaose Binding Mutated (X-2 L110F) CBM4-2 Carbohydrate Binding Module From A Thermostable Rhodothermus Marinus Xylanase, PDB code: 2y6g:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Cellopentaose Binding Mutated (X-2 L110F) CBM4-2 Carbohydrate Binding Module From A Thermostable Rhodothermus Marinus Xylanase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Cellopentaose Binding Mutated (X-2 L110F) CBM4-2 Carbohydrate Binding Module From A Thermostable Rhodothermus Marinus Xylanase within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1169 b:16.1 occ:1.00 O A:LYS55 2.2 15.3 1.0 OE1 A:GLU52 2.3 20.0 1.0 O A:GLU52 2.3 18.6 1.0 OE2 A:GLU11 2.3 17.7 1.0 OD1 A:ASP160 2.4 16.3 1.0 O A:GLY9 2.4 15.4 1.0 OD2 A:ASP160 2.6 16.0 1.0 CG A:ASP160 2.9 15.5 1.0 C A:GLU52 3.2 19.5 1.0 C A:GLY9 3.4 14.0 1.0 C A:LYS55 3.4 13.8 1.0 CD A:GLU11 3.5 19.0 1.0 CD A:GLU52 3.5 22.1 1.0 CA A:GLY9 3.7 15.2 1.0 CB A:GLU52 3.9 22.4 1.0 N A:LYS55 3.9 16.1 1.0 CG A:GLU11 4.0 19.3 1.0 CA A:GLU52 4.0 21.6 1.0 CA A:LYS55 4.2 16.6 1.0 N A:GLY53 4.2 21.9 1.0 CG A:GLU52 4.3 22.5 1.0 N A:GLU52 4.3 20.9 1.0 CA A:GLY53 4.3 23.0 1.0 CB A:ASP160 4.4 14.7 1.0 OE2 A:GLU52 4.4 35.7 1.0 N A:VAL56 4.5 14.3 1.0 C A:GLY53 4.5 21.8 1.0 N A:ASN54 4.5 21.7 1.0 OE1 A:GLU11 4.5 23.1 1.0 N A:PHE10 4.6 14.6 1.0 CB A:LYS55 4.6 17.1 1.0 CB A:ALA50 4.7 24.1 1.0 CA A:VAL56 4.8 13.1 1.0 N A:GLY161 4.9 14.0 1.0 N A:GLU11 5.0 17.4 1.0

Calcium binding site 2 out of 2 in the Cellopentaose Binding Mutated (X-2 L110F) CBM4-2 Carbohydrate Binding Module From A Thermostable Rhodothermus Marinus Xylanase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Cellopentaose Binding Mutated (X-2 L110F) CBM4-2 Carbohydrate Binding Module From A Thermostable Rhodothermus Marinus Xylanase within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1170 b:24.3 occ:0.50 O A:HOH2046 2.2 23.9 1.0 O A:HOH2050 2.3 48.4 1.0 O A:HOH2039 2.4 51.0 1.0 O A:ALA22 2.4 22.6 1.0 O A:HOH2102 2.6 29.6 1.0 O A:TRP28 2.7 15.9 1.0 C A:TRP28 3.6 12.9 1.0 C A:ALA22 3.6 19.3 1.0 O A:HOH2016 4.0 43.2 1.0 CA A:GLU23 4.1 22.4 1.0 N A:ASP29 4.2 12.7 1.0 CA A:ASP29 4.2 13.8 0.5 CA A:ASP29 4.2 13.5 0.5 O A:HOH2045 4.3 16.7 1.0 N A:GLU23 4.4 19.6 1.0 CB A:ASP29 4.4 18.4 0.5 O A:VAL25 4.4 14.8 1.0 CB A:ASP29 4.5 17.9 0.5 N A:TRP28 4.5 13.4 1.0 CG A:GLU23 4.5 36.2 1.0 O A:HOH2048 4.6 24.2 1.0 CA A:TRP28 4.6 12.8 1.0 CA A:ALA22 4.7 19.9 1.0 OD2 A:ASP29 4.7 33.5 0.5 O A:LEU76 4.8 15.7 1.0 CB A:GLU23 4.9 28.0 1.0 CG A:ASP29 4.9 22.6 0.5 OD1 A:ASP29 4.9 21.1 0.5 CD1 A:LEU76 4.9 35.2 1.0

L.Von Schantz, M.Hakansson, D.T.Logan, B.Walse, J.Osterlin, E.Nordberg-Karlsson, M.Ohlin. Structural Basis For Carbohydrate-Binding Specificity--A Comparative Assessment of Two Engineered Carbohydrate-Binding Modules. Glycobiology V. 22 948 2012.
ISSN: ESSN 1460-2423
PubMed: 22434778
DOI: 10.1093/GLYCOB/CWS063