2vhr Summary


Atomic resolution (0.95A) structure of purified thaumatin I grown in sodium L-tartrate at 4 C

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 0.95 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-1. This molecule has the UniProt identifier P02883 (THM1_THADA)search. The sample contained 207 residues which is 100% of the natural sequence. Out of 207 residues 206 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-1 P02883 (1-207) (THM1_THADA)search Thaumatococcus danielliisearch 100% 207 99%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P02883 (1 - 207) THAUMATIN-1 Thaumatococcus daniellii

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

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

Chain InterPro annotation
A Thaumatinsearch Thaumatin, conserved sitesearch