PDBe 1thu

X-ray diffraction
2.6Å resolution

THE STRUCTURES OF THREE CRYSTAL FORMS OF THE SWEET PROTEIN THAUMATIN

Released:
Source organism: Thaumatococcus daniellii
Primary publication:
Structures of three crystal forms of the sweet protein thaumatin.
Acta Crystallogr. D Biol. Crystallogr. 50 813-25 (1994)
PMID: 15299348

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thaumatin-1 Chain: A
Molecule details ›
Chain: A
Length: 207 amino acids
Theoretical weight: 22.24 KDa
Source organism: Thaumatococcus daniellii
Expression system: Not provided
UniProt:
  • Canonical: P02883 (Residues: 1-207; Coverage: 100%)
Sequence domains: Thaumatin family
Structure domains: Thaumatin

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 117.7Å b: 44.9Å c: 38Å
α: 90° β: 94° γ: 90°
R-values:
R R work R free
0.184 not available not available
Expression system: Not provided