› 3wwg

X-ray diffraction
2.2Å resolution

Crystal structure of the N-glycan-deficient variant N448A of isopullulanase complexed with isopanose

Released:
DOI: 10.2210/pdb3wwg/pdb
PDB entry 3wwg coloured by chain, front view.
PDB entry 3wwg coloured by chain, side view.
PDB entry 3wwg coloured by chain, top view.
Source organism: Aspergillus niger
Primary publication:
The side chain of a glycosylated asparagine residue is important for the stability of isopullulanase.
Miyazaki T, Yashiro H, Nishikawa A, Tonozuka T
J Biochem 157 225-34 (2015)
PMID: 25359784

Function and Biology Details

Reaction catalysed: 
Hydrolysis of pullulan to isopanose (6-alpha-maltosylglucose)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-126117 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Isopullulanase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 549 amino acids
Theoretical weight: 60 KDa
Source organism: Aspergillus niger
Expression system: Komagataella pastoris
UniProt:
  • Canonical: O00105 (Residues: 20-564; Coverage: 100%)
Gene name: ipuA
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: BGC, GLC
Carbohydrate polymer
Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
1 bound ligand:
Ligand NAG 32 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: P21
Unit cell:
a: 96.4Å b: 108.1Å c: 116Å
α: 90° β: 103.9° γ: 90°
R-values:
R R work R free
0.185 0.183 0.224
Expression system: Komagataella pastoris

Quick links

Citations

2 citation in other articles

Isolation and characterization of an aspartic protease able to hydrolyze and decolorize heme proteins from Aspergillus glaucus.
Takenaka et al. (2019)
1 more