› 1bvz

X-ray diffraction
2.6Å resolution

ALPHA-AMYLASE II (TVAII) FROM THERMOACTINOMYCES VULGARIS R-47

Released:
DOI: 10.2210/pdb1bvz/pdb
PDB entry 1bvz coloured by chain, front view.
PDB entry 1bvz coloured by chain, side view.
PDB entry 1bvz coloured by chain, top view.
Source organism: Thermoactinomyces vulgaris
Primary publication:
Crystal structure of Thermoactinomyces vulgaris R-47 alpha-amylase II (TVAII) hydrolyzing cyclodextrins and pullulan at 2.6 A resolution.
Kamitori S, Kondo S, Okuyama K, Yokota T, Shimura Y, Tonozuka T, Sakano Y
J Mol Biol 287 907-21 (1999)
PMID: 10222200

Function and Biology Details

Reaction catalysed: 
Hydrolysis of pullulan to panose (6-alpha-D-glucosylmaltose)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170688 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P212121
Unit cell:
a: 114.6Å b: 117.9Å c: 114Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.196 0.272
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Relationship of sequence and structure to specificity in the alpha-amylase family of enzymes.
MacGregor et al. (2001)
5 more

3 mentions without citation

Defining structural and evolutionary modules in proteins: a community detection approach to explore sub-domain architecture.
Hleap et al. (2013)
2 more