3pnr Summary


Structure of PbICP-C in complex with falcipain-2

The structure was published by Hansen, G., Heitmann, A., Witt, T., et al., Heussler, V.T., Rennenberg, A., and Hilgenfeld, R., in 2011 in a paper entitled "Structural basis for the regulation of cysteine-protease activity by a new class of protease inhibitors in Plasmodium." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.6 Å and deposited in 2010.

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

This PDB entry contains a complex of 2 biomacromolecules, namely Falcipain 2 and PbICP-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 most likely forms heterodimers.

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 Falcipain 2 Q9N6S8 (245-484) (Q9N6S8_PLAFA)search Plasmodium falciparumsearch < 90% 240 100%
B PbICP-C Q4YW59 (189-353) (Q4YW59_PLABA)search Plasmodium berghei ANKAsearch < 90% 187 68%

This entry contains 2 unique UniProt proteins:

UniProt accession Name Organism PDB
Q9N6S8 (245 - 484) Falcipain 2 Plasmodium falciparum
Q4YW59 (189 - 353) PbICP-C Plasmodium berghei

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

Chain ID Biological process (GO) Molecular function (GO)
A (Q9N6S8) proteolysissearch cysteine-type peptidase activitysearch

Chain InterPro annotation
A Peptidase C1A, papain C-terminalsearch Peptidase C1Asearch Cysteine peptidase, histidine active sitesearch
B Proteinase inhibitor I42, chagasinsearch Protease inhibitor, falstatinsearch