PDBe 1ly0

X-ray diffraction
1.36Å resolution

Structure of thaumatin crystallized in the presence of glycerol

Released:
Source organism: Thaumatococcus daniellii
Primary publication:
Crystallization in the presence of glycerol displaces water molecules in the structure of thaumatin.
Acta Crystallogr. D Biol. Crystallogr. 58 2060-5 (2002)
PMID: 12454465

Function and Biology Details

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

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: 22.23 KDa
Source organism: Thaumatococcus daniellii
UniProt:
  • Best match: P02883 (Residues: 1-207)

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LURE BEAMLINE DW32
Spacegroup: P41212
Unit cell:
a: 57.867Å b: 57.867Å c: 149.96Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.195 0.204