› 1e5b

Solution NMR

Internal xylan binding domain from C. fimi Xyn10A, R262G mutant

Released:
DOI: 10.2210/pdb1e5b/pdb
PDB entry 1e5b coloured by chain, front view.
PDB entry 1e5b coloured by chain, side view.
PDB entry 1e5b coloured by chain, top view.
Source organism: Cellulomonas fimi
Primary publication:
The structural basis for the ligand specificity of family 2 carbohydrate-binding modules.
Simpson PJ, Xie H, Bolam DN, Gilbert HJ, Williamson MP
J Biol Chem 275 41137-42 (2000)
PMID: 10973978

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-157117 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional xylanase/deacetylase Chain: A
Molecule details ›
Chain: A
Length: 87 amino acids
Theoretical weight: 8.69 KDa
Source organism: Cellulomonas fimi
Expression system: Escherichia coli
UniProt:
  • Canonical: P54865 (Residues: 247-333; Coverage: 15%)
Gene name: xynD
Structure domains: Immunoglobulin-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: HYBRID DISTANCE GEOMETRY/ SIMULATED ANNEALING
Expression system: Escherichia coli

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Citations

12 review citations

Carbohydrate-binding modules: fine-tuning polysaccharide recognition.
Boraston et al. (2004)
11 more

2 mentions without citation

Search for allosteric disulfide bonds in NMR structures.
Schmidt et al. (2007)
1 more