1h6x

X-ray diffraction
2.25Å 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:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-156366 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endo-1,4-beta-xylanase Y Chain: A
Molecule details ›
Chain: A
Length: 170 amino acids
Theoretical weight: 18.91 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:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P43212
Unit cell:
a: 38.68Å b: 38.68Å c: 207.53Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.214 0.214 0.26
Expression system: Escherichia coli BL21