2b1n Summary


Crystal structure of a papain-fold protein without the catalytic cysteine from seeds of Pachyrhizus erosus

The structure was published by Zhang, M., Wei, Z., Chang, S., Teng, M., and Gong, W., in 2006 in a paper entitled "Crystal structure of a papain-fold protein without the catalytic residue: a novel member in the cysteine proteinase family" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.4 Å and deposited in 2005.

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

This PDB entry contains a complex of 2 biomacromolecules, namely SPE31 and peptide (LYS)(ALA)(SER)(VAL)(GLY).

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 SPE31 Q3Y6U7 (1-246) (Q3Y6U7_9FABA)search Pachyrhizus erosussearch 100% 246 92%
B peptide (LYS)(ALA)(SER)(VAL)(GLY) Not available
Synthetic Not available 5 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q3Y6U7 (1 - 246) SPE31 Pachyrhizus erosus

Chain Structural classification (CATH) Sequence family (Pfam)
A (Q3Y6U7) Cysteine proteinasessearch PF00112: Papain family cysteine proteasesearch

Chain ID Molecular function (GO) Biological process (GO)
A (Q3Y6U7) cysteine-type peptidase activitysearch proteolysissearch

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