› 1b3v

X-ray diffraction
2.4Å resolution

XYLANASE FROM PENICILLIUM SIMPLICISSIMUM, COMPLEX WITH XYLOSE

Released:
DOI: 10.2210/pdb1b3v/pdb
PDB entry 1b3v coloured by chain, front view.
PDB entry 1b3v coloured by chain, side view.
PDB entry 1b3v coloured by chain, top view.
Source organism: Penicillium simplicissimum
Primary publication:
Xylan binding subsite mapping in the xylanase from Penicillium simplicissimum using xylooligosaccharides as cryo-protectant.
Schmidt A, Gübitz GM, Kratky C
Biochemistry 38 2403-12 (1999)
PMID: 10029534

Function and Biology Details

Reaction catalysed: 
Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157498 (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

2 bound ligands:
Ligand XYP 3 x XYP
Ligand XYS 1 x XYS
1 modified residue:
Ligand PCA 1 x PCA

Experiments and Validation Details

Entry percentile scores
X-ray source: SIEMENS
Spacegroup: P3121
Unit cell:
a: 81.86Å b: 81.86Å c: 113.59Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.211 0.211 0.274

Quick links

Citations

6 review citations

Structural determinants of the substrate specificities of xylanases from different glycoside hydrolase families.
Pollet et al. (2010)
5 more

1 mention without citation

Using Carbohydrate Interaction Assays to Reveal Novel Binding Sites in Carbohydrate Active Enzymes.
Cockburn et al. (2016)