› 1heh

Solution NMR

C-terminal xylan binding domain from Cellulomonas fimi xylanase 11A

Released:
DOI: 10.2210/pdb1heh/pdb
PDB entry 1heh coloured by chain, front view.
PDB entry 1heh coloured by chain, side view.
PDB entry 1heh coloured by chain, top view.
Source organism: Cellulomonas fimi
Primary publication:
Evidence for synergy between family 2b carbohydrate binding modules in Cellulomonas fimi xylanase 11A.
Bolam DN, Xie H, White P, Simpson PJ, Hancock SM, Williamson MP, Gilbert HJ
Biochemistry 40 2468-77 (2001)
PMID: 11327868

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: C
Molecule details ›
Chain: C
Length: 88 amino acids
Theoretical weight: 8.75 KDa
Source organism: Cellulomonas fimi
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P54865 (Residues: 557-644; 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
Chemical shift assignment: 62%
Refinement method: HYBRID DISTANCE GEOMETRY/ SIMULATED ANNEALING
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

Biotechnology of microbial xylanases: enzymology, molecular biology, and application.
Subramaniyan et al. (2002)
5 more

2 mentions without citation

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