› 1thw

X-ray diffraction
1.75Å resolution

THE STRUCTURES OF THREE CRYSTAL FORMS OF THE SWEET PROTEIN THAUMATIN

Released:
DOI: 10.2210/pdb1thw/pdb
PDB entry 1thw coloured by chain, front view.
PDB entry 1thw coloured by chain, side view.
PDB entry 1thw coloured by chain, top view.
Source organism: Thaumatococcus daniellii
Primary publication:
Structures of three crystal forms of the sweet protein thaumatin.
Ko TP, Day J, Greenwood A, McPherson A
Acta Crystallogr D Biol Crystallogr 50 813-25 (1994)
PMID: 15299348

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136332 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thaumatin I 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: 23-229; Coverage: 97%)
Sequence domains: Thaumatin family
Structure domains: Thaumatin

Ligands and Environments

1 bound ligand:
Ligand TLA 1 x TLA
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P41212
Unit cell:
a: 58.6Å b: 58.6Å c: 151.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 not available not available
Expression system: Not provided

Quick links

Citations

3 review citations

Protein folds in the all-beta and all-alpha classes.
Chothia et al. (1997)
2 more

14 mentions without citation

What role do surfaces play in GB models? A new-generation of surface-generalized born model based on a novel gaussian surface for biomolecules.
Yu et al. (2006)
13 more