3tnx Summary


Structure of the precursor of a thermostable variant of papain at 2.6 Angstroem resolution

The structure was published by Roy, S., Choudhury, D., Aich, P., Dattagupta, J.K., and Biswas, S., in 2012 in a paper entitled "The structure of a thermostable mutant of pro-papain reveals its activation mechanism" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.62 Å and deposited in 2011.

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

This PDB entry contains multiple copies of the structure of Papain.

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 Papain P00784 (27-345) (PAPA1_CARPA)search Carica papayasearch 98% 363 85%
C Papain P00784 (27-345) (PAPA1_CARPA)search Carica papayasearch 98% 363 85%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P00784 (27 - 345) Papain Carica papaya

Chain Structural classification (CATH) Sequence family (Pfam)
A, C (P00784) Cysteine proteinasessearch PF00112: Papain family cysteine proteasesearch, PF08246: Cathepsin propeptide inhibitor domain (I29)search

Chain ID Molecular function (GO) Biological process (GO)
A, C (P00784) cysteine-type peptidase activitysearch peptidase activitysearch hydrolase activitysearch proteolysissearch

Chain InterPro annotation
A, C Peptidase C1A, papain C-terminalsearch Peptidase C1Asearch Proteinase inhibitor I29, cathepsin propeptidesearch Cysteine peptidase, histidine active sitesearch Cysteine peptidase, asparagine active sitesearch