2g4y Summary


structure of thaumatin at 2.0 A wavelength

The structure was published by Mueller-Dieckmann, C., Panjikar, S., Schmidt, A., et al., Singh, R.K., Tucker, P.A., and Weiss, M.S., in 2007 in a paper entitled "On the routine use of soft X-rays in macromolecular crystallography. Part IV. Efficient determination of anomalous substructures in biomacromolecules using longer X-ray wavelengths." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.98 Å and deposited in 2006.

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 Q8RVT0 (Q8RVT0_THADA)search. The sample contained 207 residues which is 100% of the natural sequence. Out of 207 residues 207 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 Q8RVT0 (1-207) (Q8RVT0_THADA)search Thaumatococcus danielliisearch 100% 207 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q8RVT0 (1 - 207) Thaumatin-1 Thaumatococcus daniellii

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P02883)
Chain InterPro annotation
A Thaumatinsearch Thaumatin, conserved sitesearch