2i0w

X-ray diffraction
2.5Å resolution

Crystal structure analysis of NP24-I, a thaumatin-like protein

Released:
Model geometry
Fit model/data
Source organism: Solanum lycopersicum
Primary publication:
Crystal structure analysis of NP24-I: a thaumatin-like protein.
Planta 228 883-90 (2008)
PMID: 18651170

Function and Biology Details

Reaction catalysed:
Endohydrolysis of (1->3)- or (1->4)-linkages in beta-D-glucans when the glucose residue whose reducing group is involved in the linkage to be hydrolyzed is itself substituted at C-3.
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-146296 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Osmotin-like protein NP24-I Chain: A
Molecule details ›
Chain: A
Length: 207 amino acids
Theoretical weight: 22.23 KDa
Source organism: Solanum lycopersicum
UniProt:
  • Canonical: P12670 (Residues: 22-228; Coverage: 92%)
Gene names: NP24-I, Solyc08g080650
Sequence domains: Thaumatin family
Structure domains: Thaumatin

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ENRAF-NONIUS FR591
Spacegroup: P43
Unit cell:
a: 61.01Å b: 61.01Å c: 62.895Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.171 0.171 0.223