1gkk

X-ray diffraction
1.6Å resolution

Feruloyl esterase domain of XynY from clostridium thermocellum

Released:

Function and Biology Details

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

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 297 amino acids
Theoretical weight: 34.27 KDa
Source organism: Acetivibrio thermocellus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P51584 (Residues: 792-1077; Coverage: 27%)
Gene name: xynY
Sequence domains: Putative esterase
Structure domains: alpha/beta hydrolase

Ligands and Environments

2 bound ligands:
2 modified residues:

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P212121
Unit cell:
a: 65.381Å b: 108.793Å c: 113.877Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.155 0.154 0.173
Expression system: Escherichia coli BL21(DE3)