1thw Summary

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THE STRUCTURES OF THREE CRYSTAL FORMS OF THE SWEET PROTEIN THAUMATIN

The structure was published by Ko, T.P., Day, J., Greenwood, A., and McPherson, A., in 1994 in a paper entitled "Structures of three crystal forms of the sweet protein thaumatin." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.75 Å and deposited in 1994.

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

The PDB entry contains the structure of THAUMATIN. 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 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 most likely forms homodimers.

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 P02883 (1-207) (THM1_THADA)search Thaumatococcus danielliisearch 100% 207 100%


This entry contains 1 unique UniProt protein:

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

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P02883) Osmotin, thaumatin-like proteinsearch 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