› 3aok

X-ray diffraction
1.27Å resolution

Crystal structure of sweet-tasting protein thaumatin II

Released:
DOI: 10.2210/pdb3aok/pdb
PDB entry 3aok coloured by chain, front view.
PDB entry 3aok coloured by chain, side view.
PDB entry 3aok coloured by chain, top view.
Source organism: Thaumatococcus daniellii
Primary publication:
Crystal structure of the sweet-tasting protein thaumatin II at 1.27Å.
Masuda T, Ohta K, Tani F, Mikami B, Kitabatake N
Biochem Biophys Res Commun 410 457-60 (2011)
PMID: 21672520

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136333 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thaumatin II Chain: A
Molecule details ›
Chain: A
Length: 207 amino acids
Theoretical weight: 22.31 KDa
Source organism: Thaumatococcus daniellii
UniProt:
  • Canonical: P02884 (Residues: 23-229; Coverage: 97%)
Sequence domains: Thaumatin family
Structure domains: Thaumatin

Ligands and Environments

2 bound ligands:
Ligand TLA 2 x TLA
Ligand GOL 4 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: P41212
Unit cell:
a: 57.769Å b: 57.769Å c: 150.126Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.111 not available 0.148

Quick links

Citations

8 citation in other articles

Five amino acid residues in cysteine-rich domain of human T1R3 were involved in the response for sweet-tasting protein, thaumatin.
Masuda et al. (2013)
7 more

2 mentions without citation

In-vacuum long-wavelength macromolecular crystallography.
Wagner et al. (2016)
1 more