2d2o

X-ray diffraction
2.1Å resolution

Structure of a complex of Thermoactinomyces vulgaris R-47 alpha-amylase 2 with maltohexaose demonstrates the important role of aromatic residues at the reducing end of the substrate binding cleft

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Neopullulanase 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 585 amino acids
Theoretical weight: 67.55 KDa
Source organism: Thermoactinomyces vulgaris
Expression system: Escherichia coli
UniProt:
  • Canonical: Q08751 (Residues: 1-585; Coverage: 100%)
Gene name: tvaII
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: SPRING-8 BEAMLINE BL44XU
Spacegroup: P212121
Unit cell:
a: 113.69Å b: 118.71Å c: 112.38Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.184 0.217
Expression system: Escherichia coli