1ppd Summary

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RESTRAINED LEAST-SQUARES REFINEMENT OF THE SULFHYDRYL PROTEASE PAPAIN TO 2.0 ANGSTROMS

The structure was published by Priestle, J.P., Ford, G.C., Glor, M., et al., Smit, J.D.G., Thaller, C., and Jansonius, J.N., in 1984 in a paper entitled "Restrained Least-Squares Refinement of the Sulfhydryl Protease Papain to 2.0 Angstroms" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 1984.

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

The PDB entry contains the structure of 2-HYDROXYETHYL-THIOPAPAIN. This molecule has the UniProt identifier P00784 (PAPA1_CARPA)search. The sample contained 212 residues which is < 90% of the natural sequence. Out of 212 residues 212 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 2-HYDROXYETHYL-THIOPAPAIN P00784 (134-345) (PAPA1_CARPA)search Carica papayasearch 98% 212 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P00784 (134 - 345) 2-HYDROXYETHYL-THIOPAPAIN Carica papaya

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P00784) Papain-likesearch Cysteine proteinasessearch PF00112: Papain family cysteine proteasesearch

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

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