3wdj

X-ray diffraction
2.22Å resolution

Crystal structure of Pullulanase complexed with maltotetraose from Anoxybacillus sp. LM18-11

Released:
Source organism: Anoxybacillus sp. LM18-11
Entry authors: Xu J, Ren F, Huang CH, Zheng Y, Zhen J, Ko TP, Chen CC, Chan HC, Guo RT, Ma Y, Song H

Function and Biology Details

Reaction catalysed:
Hydrolysis of (1->6)-alpha-D-glucosidic linkages in pullulan, amylopectin and glycogen, and in the alpha- and beta-limit dextrins of amylopectin and glycogen.
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-125644 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
pullulanase Chain: A
Molecule details ›
Chain: A
Length: 710 amino acids
Theoretical weight: 82.17 KDa
Source organism: Anoxybacillus sp. LM18-11
Expression system: Escherichia coli
UniProt:
  • Canonical: K9L0H1 (Residues: 3-707; Coverage: 100%)
Gene name: pulA
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13B1
Spacegroup: P21212
Unit cell:
a: 139.971Å b: 65.929Å c: 90.921Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.181 0.217
Expression system: Escherichia coli