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Sodium in PDB 2qz2: Crystal Structure of A Glycoside Hydrolase Family 11 Xylanase From Aspergillus Niger in Complex with Xylopentaose

Enzymatic activity of Crystal Structure of A Glycoside Hydrolase Family 11 Xylanase From Aspergillus Niger in Complex with Xylopentaose

All present enzymatic activity of Crystal Structure of A Glycoside Hydrolase Family 11 Xylanase From Aspergillus Niger in Complex with Xylopentaose:
3.2.1.8;

Protein crystallography data

The structure of Crystal Structure of A Glycoside Hydrolase Family 11 Xylanase From Aspergillus Niger in Complex with Xylopentaose, PDB code: 2qz2 was solved by E.Vandermarliere, S.Rombouts, S.V.Strelkov, J.A.Delcour, C.M.Courtin, A.Rabijns, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.48 / 2.80
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 67.326, 67.326, 165.401, 90.00, 90.00, 120.00
R / Rfree (%) 22.1 / 27.7

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of A Glycoside Hydrolase Family 11 Xylanase From Aspergillus Niger in Complex with Xylopentaose (pdb code 2qz2). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Crystal Structure of A Glycoside Hydrolase Family 11 Xylanase From Aspergillus Niger in Complex with Xylopentaose, PDB code: 2qz2:

Sodium binding site 1 out of 1 in 2qz2

Go back to Sodium Binding Sites List in 2qz2
Sodium binding site 1 out of 1 in the Crystal Structure of A Glycoside Hydrolase Family 11 Xylanase From Aspergillus Niger in Complex with Xylopentaose


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of A Glycoside Hydrolase Family 11 Xylanase From Aspergillus Niger in Complex with Xylopentaose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na1141

b:18.5
occ:1.00
 O A:SER183 2.4 22.0 1.0
O A:HOH1157 2.6 18.9 1.0
C A:SER183 3.6 22.0 1.0
N A:THR53 3.6 21.7 1.0
O A:THR53 4.1 22.5 1.0
CA A:ILE52 4.1 21.1 1.0
O A:ALA51 4.2 20.8 1.0
CG2 A:ILE182 4.2 22.0 1.0
CZ2 A:TRP44 4.4 20.2 1.0
CH2 A:TRP44 4.4 20.1 1.0
C A:ILE52 4.4 21.3 1.0
CG2 A:ILE52 4.5 21.1 1.0
CA A:THR53 4.5 22.1 1.0
CA A:SER183 4.6 22.0 1.0
N A:SER183 4.6 22.0 1.0
CB A:THR53 4.7 22.1 1.0
C A:THR53 4.8 22.5 1.0
CB A:ILE52 4.8 21.0 1.0

Reference:

E.Vandermarliere, T.M.Bourgois, S.Rombouts, S.Van Campenhout, G.Volckaert, S.V.Strelkov, J.A.Delcour, A.Rabijns, C.M.Courtin. Crystallographic Analysis Shows Substrate Binding at the -3 to +1 Active-Site Subsites and at the Surface of Glycoside Hydrolase Family 11 Endo-1,4-Beta-Xylanases. Biochem.J. V. 410 71 2008.
ISSN: ISSN 0264-6021
PubMed: 17983355
DOI: 10.1042/BJ20071128
Page generated: Mon Oct 7 04:06:18 2024

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