› 1y4w

X-ray diffraction
1.55Å resolution

Crystal structure of exo-inulinase from Aspergillus awamori in spacegroup P21

Released:
DOI: 10.2210/pdb1y4w/pdb
PDB entry 1y4w coloured by chain, front view.
PDB entry 1y4w coloured by chain, side view.
PDB entry 1y4w coloured by chain, top view.
Source organism: Aspergillus awamori
Primary publication:
Crystal structure of exo-inulinase from Aspergillus awamori: the enzyme fold and structural determinants of substrate recognition.
Nagem RA, Rojas AL, Golubev AM, Korneeva OS, Eneyskaya EV, Kulminskaya AA, Neustroev KN, Polikarpov I
J Mol Biol 344 471-80 (2004)
PMID: 15522299

Function and Biology Details

Reaction catalysed: 
Hydrolysis of terminal, non-reducing (2->1)- and (2->6)-linked beta-D-fructofuranose residues in fructans
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188773 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Extracellular exo-inulinase inuE Chain: A
Molecule details ›
Chain: A
Length: 518 amino acids
Theoretical weight: 57.19 KDa
Source organism: Aspergillus awamori
UniProt:
  • Canonical: Q96TU3 (Residues: 20-537; Coverage: 100%)
Gene names: inu1, inuE
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
2 bound ligands:
Ligand NAG 3 x NAG
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU ULTRAX 18
Spacegroup: P21
Unit cell:
a: 49.954Å b: 94.029Å c: 67.634Å
α: 90° β: 107.04° γ: 90°
R-values:
R R work R free
0.171 0.17 0.198

Quick links

Citations

11 review citations

Structural insights into glycoside hydrolase family 32 and 68 enzymes: functional implications.
Lammens et al. (2009)
10 more

7 mentions without citation

Structural and kinetic analysis of Schwanniomyces occidentalis invertase reveals a new oligomerization pattern and the role of its supplementary domain in substrate binding.
Alvaro-Benito et al. (2010)
6 more