› 1h6y

X-ray diffraction
2.2Å resolution

The role of conserved amino acids in the cleft of the C-terminal family 22 carbohydrate binding module of Clostridium thermocellum Xyn10B in ligand binding

Released:
DOI: 10.2210/pdb1h6y/pdb
PDB entry 1h6y coloured by chain, front view.
PDB entry 1h6y coloured by chain, side view.
PDB entry 1h6y coloured by chain, top view.
Source organism: Acetivibrio thermocellus
Primary publication:
Clostridium thermocellum Xyn10B carbohydrate-binding module 22-2: the role of conserved amino acids in ligand binding.
Xie H, Gilbert HJ, Charnock SJ, Davies GJ, Williamson MP, Simpson PJ, Raghothama S, Fontes CM, Dias FM, Ferreira LM, Bolam DN
Biochemistry 40 9167-76 (2001)
PMID: 11478884

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156366 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endo-1,4-beta-xylanase Y Chains: A, B
Molecule details ›
Chains: A, B
Length: 170 amino acids
Theoretical weight: 18.94 KDa
Source organism: Acetivibrio thermocellus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P51584 (Residues: 560-720; Coverage: 15%)
Gene name: xynY
Sequence domains: Carbohydrate binding domain
Structure domains: Galactose-binding domain-like

Ligands and Environments

1 bound ligand:
Ligand CA 2 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P6122
Unit cell:
a: 89.869Å b: 89.869Å c: 209.003Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.194 0.194 0.228
Expression system: Escherichia coli BL21

Quick links

Citations

4 review citations

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

3 mentions without citation

Discovery of a Thermostable GH10 Xylanase with Broad Substrate Specificity from the Arctic Mid-Ocean Ridge Vent System.
Fredriksen et al. (2019)
2 more