2pre Summary


Crystal structure of plant cysteine protease Ervatamin-C complexed with irreversible inhibitor E-64 at 2.7 A resolution

The structure was published by Ghosh, R., Chakraborty, S., Chakrabarti, C., Dattagupta, J.K., and Biswas, S., in 2008 in a paper entitled "Structural insights into the substrate specificity and activity of ervatamins, the papain-like cysteine proteases from a tropical plant, Ervatamia coronaria." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.7 Å and deposited in 2007.

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

This PDB entry contains multiple copies of the structure of Ervatamin-C.

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 has more than one probable quaternary state observed. For more details see the quaternary structure page.

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 Ervatamin-C A8DS38 (134-341) (A8DS38_TABDI)search Tabernaemontana divaricatasearch < 90% 208 100%
B Ervatamin-C A8DS38 (134-341) (A8DS38_TABDI)search Tabernaemontana divaricatasearch < 90% 208 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
A8DS38 (134 - 341) Ervatamin-C Tabernaemontana divaricata

Chain Structural classification (CATH) Sequence family (Pfam)
A, B Cysteine proteinasessearch Papain family cysteine proteasesearch

Chain ID Molecular function (GO) Biological process (GO)
A, B (A8DS38) cysteine-type peptidase activitysearch proteolysissearch

Chain InterPro annotation
A, B Cysteine peptidase, cysteine active sitesearch Peptidase C1A, papain C-terminalsearch Peptidase C1Asearch Cysteine peptidase, asparagine active sitesearch