2oz2 Summary


Crystal structure analysis of cruzain bound to vinyl sulfone derived inhibitor (K11777)

The structure was published by Kerr, I.D., Lee, J.H., Farady, C.J., et al., Craik, C.S., Rosenthal, P.J., and Brinen, L.S., in 2009 in a paper entitled "Vinyl sulfones as antiparasitic agents and a structural basis for drug design." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.95 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 Cruzipain.

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 Cruzipain P25779 (123-337) (CYSP_TRYCR)search Trypanosoma cruzisearch < 90% 215 100%
C Cruzipain P25779 (123-337) (CYSP_TRYCR)search Trypanosoma cruzisearch < 90% 215 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P25779 (123 - 337) Cruzipain Trypanosoma cruzi

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, C Papain-likesearch Cysteine proteinasessearch Papain family cysteine proteasesearch, Protein of unknown function (DUF3586)search

Chain ID Molecular function (GO) Biological process (GO)
A, C (P25779) cysteine-type peptidase activitysearch proteolysissearch

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