2vhk Summary

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ATOMIC RESOLUTION (0.94 A) STRUCTURE OF PURIFIED THAUMATIN I GROWN IN SODIUM L-TARTRATE AT 22C

The structure was published by Asherie, N., Jakoncic, J., Ginsberg, C., et al., Hrnjez, B.J., Blass, S., and Berger, J., in 2009 in a paper entitled "Tartrate Chirality Determines Thaumatin Crystal Habit" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 0.94 Å and deposited in 2007.

The experimental data on which the structure is based was also deposited.

The PDB entry contains the structure of THAUMATIN-I. This molecule has the UniProt identifier P02883 (THM1_THADA)search. The sample contained 206 residues which is 100% of the natural sequence. Out of 206 residues 205 were observed and are deposited in the PDB.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule is most likely monomeric.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A THAUMATIN-I P02883 (1-206) (THM1_THADA)search Thaumatococcus danielliisearch 100% 206 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P02883 (1 - 206) THAUMATIN-I Thaumatococcus daniellii

Chain Structural classification (CATH) Sequence family (Pfam)
A (P02883) Thaumatinsearch PF00314: Thaumatin familysearch

Chain ID Cellular component (GO)
A (P02883) cytoplasmic membrane-bounded vesiclesearch cytoplasmic vesiclesearch

Chain InterPro annotation
A Thaumatinsearch Thaumatin, conserved sitesearch