› 1w3h

X-ray diffraction
1.5Å resolution

The 3-dimensional structure of a thermostable mutant of a xylanase (Xyn10A) from Cellvibrio japonicus

Released:
DOI: 10.2210/pdb1w3h/pdb
PDB entry 1w3h coloured by chain, front view.
PDB entry 1w3h coloured by chain, side view.
PDB entry 1w3h coloured by chain, top view.
Source organism: Cellvibrio japonicus
Primary publication:
The use of forced protein evolution to investigate and improve stability of family 10 xylanases. The production of Ca2+-independent stable xylanases.
Andrews SR, Taylor EJ, Pell G, Vincent F, Ducros VM, Davies GJ, Lakey JH, Gilbert HJ
J Biol Chem 279 54369-79 (2004)
PMID: 15452124

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-147071 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endo-1,4-beta-xylanase A Chains: A, B
Molecule details ›
Chains: A, B
Length: 359 amino acids
Theoretical weight: 39.84 KDa
Source organism: Cellvibrio japonicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P14768 (Residues: 265-611; Coverage: 59%)
Gene names: CJA_2471, xyn10A, xynA
Sequence domains: Glycosyl hydrolase family 10
Structure domains: Glycosidases

Ligands and Environments

2 bound ligands:
Ligand CA 2 x CA
Ligand EDO 2 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P43212
Unit cell:
a: 95.232Å b: 95.232Å c: 151.784Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.218 0.217 0.251
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Starch and alpha-glucan acting enzymes, modulating their properties by directed evolution.
Kelly et al. (2009)
4 more