› 1uh2

X-ray diffraction
2Å resolution

Thermoactinomyces vulgaris R-47 alpha-amylase/malto-hexaose complex

Released:
DOI: 10.2210/pdb1uh2/pdb
PDB entry 1uh2 coloured by chain, front view.
PDB entry 1uh2 coloured by chain, side view.
PDB entry 1uh2 coloured by chain, top view.
Source organism: Thermoactinomyces vulgaris
Primary publication:
Complex structures of Thermoactinomyces vulgaris R-47 alpha-amylase 1 with malto-oligosaccharides demonstrate the role of domain N acting as a starch-binding domain.
Abe A, Tonozuka T, Sakano Y, Kamitori S
J Mol Biol 335 811-22 (2004)
PMID: 14687576

Function and Biology Details

Reaction catalysed: 
Hydrolysis of pullulan to panose (6-alpha-D-glucosylmaltose)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-178752 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Neopullulanase 1 Chain: A
Molecule details ›
Chain: A
Length: 637 amino acids
Theoretical weight: 71.11 KDa
Source organism: Thermoactinomyces vulgaris
Expression system: Escherichia coli
UniProt:
  • Canonical: Q60053 (Residues: 30-666; Coverage: 100%)
Gene name: tvaI
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
1 bound ligand:
Ligand CA 3 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: C2
Unit cell:
a: 121.63Å b: 50.491Å c: 108.015Å
α: 90° β: 103.82° γ: 90°
R-values:
R R work R free
0.184 0.184 0.217
Expression system: Escherichia coli

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Citations

11 review citations

Carbohydrate-binding modules: fine-tuning polysaccharide recognition.
Boraston et al. (2004)
10 more