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Calcium in PDB 2y6j: X-2 Engineered Mutated CBM4-2 Carbohydrate Binding Module From A Thermostable Rhodothermus Marinus Xylanase

Enzymatic activity of X-2 Engineered Mutated CBM4-2 Carbohydrate Binding Module From A Thermostable Rhodothermus Marinus Xylanase

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

Protein crystallography data

The structure of X-2 Engineered Mutated CBM4-2 Carbohydrate Binding Module From A Thermostable Rhodothermus Marinus Xylanase, PDB code: 2y6j 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) 17.00 / 1.70
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 48.360, 49.680, 62.150, 90.00, 90.00, 90.00
R / Rfree (%) 15.3 / 20.1

Calcium Binding Sites:

The binding sites of Calcium atom in the X-2 Engineered Mutated CBM4-2 Carbohydrate Binding Module From A Thermostable Rhodothermus Marinus Xylanase (pdb code 2y6j). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the X-2 Engineered Mutated CBM4-2 Carbohydrate Binding Module From A Thermostable Rhodothermus Marinus Xylanase, PDB code: 2y6j:

Calcium binding site 1 out of 1 in 2y6j

Go back to Calcium Binding Sites List in 2y6j
Calcium binding site 1 out of 1 in the X-2 Engineered Mutated 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 X-2 Engineered Mutated 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:22.0
occ:0.80
 O A:LYS55 2.2 18.5 1.0
O A:GLU52 2.3 28.9 1.0
OD1 A:ASP160 2.3 19.7 1.0
O A:GLY9 2.3 19.5 1.0
O A:HOH2086 2.6 32.6 1.0
OD2 A:ASP160 2.9 20.6 1.0
O A:HOH2018 2.9 25.9 1.0
CG A:ASP160 2.9 17.8 1.0
C A:GLU52 3.2 29.8 1.0
C A:GLY9 3.3 18.1 1.0
C A:LYS55 3.4 19.2 1.0
CA A:GLY9 3.5 17.3 1.0
N A:LYS55 3.9 22.8 1.0
CB A:GLU52 3.9 30.0 1.0
CA A:GLU52 4.0 29.8 1.0
CA A:LYS55 4.1 21.3 1.0
N A:GLY53 4.2 29.1 1.0
N A:GLU52 4.2 30.0 1.0
CB A:ASP160 4.3 15.6 1.0
CG A:GLU11 4.4 23.6 1.0
N A:VAL56 4.4 17.2 1.0
CA A:GLY53 4.5 28.8 1.0
CG A:GLU52 4.5 31.3 1.0
C A:GLY53 4.5 28.4 1.0
N A:PHE10 4.5 17.0 1.0
CB A:ALA50 4.6 32.2 1.0
N A:ASN54 4.7 27.6 1.0
CA A:VAL56 4.7 15.9 1.0
CB A:LYS55 4.7 21.4 1.0
CG1 A:VAL56 4.9 16.4 1.0
CD2 A:PHE10 4.9 14.5 1.0
N A:GLY161 4.9 14.2 1.0
O A:GLY53 5.0 28.6 1.0
C A:ASN54 5.0 25.0 1.0
CB A:PHE10 5.0 17.2 1.0

Reference:

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
Page generated: Fri Jul 12 19:25:11 2024

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