1JQP

dipeptidyl peptidase I (cathepsin C), a tetrameric cysteine protease of the papain family

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.40 Å
  • R-Value Free: 0.274 
  • R-Value Work: 0.245 

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This is version 1.4 of the entry. See complete history. 


Literature

Tetrameric dipeptidyl peptidase I directs substrate specificity by use of the residual pro-part domain

Olsen, J.G., Kadziola, A., Lauritzen, C., Pedersen, J., Larsen, S., Dahl, S.W.

(2001) FEBS Lett 506: 201-206

  • DOI: https://doi.org/10.1016/s0014-5793(01)02911-8
  • Primary Citation of Related Structures:  
    1JQP

  • PubMed Abstract: 

    The crystal structure of mature dipeptidyl peptidase I reveals insight into the unique tetrameric structure, substrate binding and activation of this atypical papain family peptidase. Each subunit is composed of three peptides. The heavy and light chains form the catalytic domain, which adopts the papain fold. The residual pro-part forms a beta-barrel with the carboxylate group of Asp1 pointing towards the substrate amino-terminus. The tetrameric structure appears to stabilize the association of the two domains and encloses a 12700 A3 spherical cavity. The tetramer contains six chloride ions, one buried in each S2 pocket and two at subunit interfaces.

    • Organizational Affiliation: 

    Center for Crystallographic Studies, University of Copenhagen, Denmark.


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
dipeptidyl peptidase I438Rattus norvegicusMutation(s): 0 
EC: 3.4.14.1
UniProt
Find proteins for P80067 (Rattus norvegicus)
Explore P80067 
Go to UniProtKB:  P80067
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP80067
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.40 Å
  • R-Value Free: 0.274 
  • R-Value Work: 0.245 
  • Space Group: P 64 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 166.24α = 90
b = 166.24β = 90
c = 80.48γ = 120
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
CNSrefinement
CNSphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2002-10-18
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Derived calculations, Version format compliance
  • Version 1.3: 2018-02-14
    Changes: Data collection, Experimental preparation
  • Version 1.4: 2020-07-29
    Type: Remediation
    Reason: Carbohydrate remediation
    Changes: Data collection, Database references, Derived calculations, Structure summary