› 1uqy

X-ray diffraction
1.72Å resolution

Xylanase Xyn10B mutant (E262S) from Cellvibrio mixtus in complex with xylopentaose

Released:
DOI: 10.2210/pdb1uqy/pdb
PDB entry 1uqy coloured by chain, front view.
PDB entry 1uqy coloured by chain, side view.
PDB entry 1uqy coloured by chain, top view.
Source organism: Cellvibrio mixtus
Primary publication:
The mechanisms by which family 10 glycoside hydrolases bind decorated substrates.
Pell G, Taylor EJ, Gloster TM, Turkenburg JP, Fontes CM, Ferreira LM, Nagy T, Clark SJ, Davies GJ, Gilbert HJ
J Biol Chem 279 9597-605 (2004)
PMID: 14668328

Function and Biology Details

Reaction catalysed: 
Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130618 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Beta-xylanase Chain: A
Molecule details ›
Chain: A
Length: 378 amino acids
Theoretical weight: 42.95 KDa
Source organism: Cellvibrio mixtus
Expression system: Escherichia coli
UniProt:
  • Canonical: O68541 (Residues: 11-379; Coverage: 97%)
Gene name: xynC
Sequence domains: Glycosyl hydrolase family 10
Structure domains: Glycosidases

Ligands and Environments

Carbohydrate polymer : NEW Components: XYS, XYP
Carbohydrate polymer
Carbohydrate polymer : NEW Components: XYP
Carbohydrate polymer
1 bound ligand:
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 47.158Å b: 67.901Å c: 104.794Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.142 0.14 0.186
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Xylanases, xylanase families and extremophilic xylanases.
Collins et al. (2005)
6 more

13 mentions without citation

Structural insights into the specificity of Xyn10B from Paenibacillus barcinonensis and its improved stability by forced protein evolution.
Gallardo et al. (2010)
12 more