2aim Summary

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CRUZAIN INHIBITED WITH BENZOYL-ARGININE-ALANINE-FLUOROMETHYLKETONE

The structure was published by Gillmor, S.A., Craik, C.S., and Fletterick, R.J., in 1997 in a paper entitled "Structural determinants of specificity in the cysteine protease cruzain." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.2 Å and deposited in 1997.

The experimental data on which the structure is based was not deposited.

The PDB entry contains the structure of CRUZAIN. This molecule has the UniProt identifier P25779 (CYSP_TRYCR)search. The sample contained 215 residues which is < 90% of the natural sequence. Out of 215 residues 215 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 CRUZAIN 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) CRUZAIN Trypanosoma cruzi

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

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

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