1xkg Summary

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Crystal structure of the major house dust mite allergen Der p 1 in its pro form at 1.61 A resolution

The structure was published by Meno, K., Thorsted, P.B., Ipsen, H., et al., Spangfort, M.D., Gajhede, M., and Lund, K., in 2005 in a paper entitled "The crystal structure of recombinant proDer p 1, a major house dust mite proteolytic allergen." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.61 Å and deposited in 2004.

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

The PDB entry contains the structure of Major mite fecal allergen Der p 1. This molecule has the UniProt identifier P08176 (PEPT1_DERPT)search. The sample contained 312 residues which is 100% of the natural sequence. Out of 312 residues 298 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 Major mite fecal allergen Der p 1 P08176 (19-320) (PEPT1_DERPT)search Dermatophagoides pteronyssinussearch 100% 312 95%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P08176 (19 - 320) Major mite fecal allergen Der p 1 Dermatophagoides pteronyssinus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P08176) Papain-likesearch Cysteine proteinasessearch PF00112: Papain family cysteine proteasesearch

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
A (P08176) cysteine-type peptidase activitysearch hydrolase activitysearch peptidase activitysearch proteolysissearch extracellular regionsearch

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