PDBe 1b31

X-ray diffraction
1.75Å resolution

XYLANASE FROM PENICILLIUM SIMPLICISSIMUM, NATIVE WITH PEG200 AS CRYOPROTECTANT

Released:

Function and Biology Details

Reaction catalysed:
Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans. 

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endo-1,4-beta-xylanase Chain: A
Molecule details ›
Chain: A
Length: 302 amino acids
Theoretical weight: 32.57 KDa
Source organism: Penicillium simplicissimum
UniProt:
  • Canonical: P56588 (Residues: 1-302; Coverage: 100%)
Sequence domains: Glycosyl hydrolase family 10
Structure domains: Glycosidases

Ligands and Environments

No bound ligands

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P3121
Unit cell:
a: 81.188Å b: 81.188Å c: 113.042Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.213 0.213 0.243