1MIR

RAT PROCATHEPSIN B


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.80 Å
  • R-Value Free: 0.270 
  • R-Value Work: 0.220 
  • R-Value Observed: 0.220 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Structure of rat procathepsin B: model for inhibition of cysteine protease activity by the proregion.

Cygler, M.Sivaraman, J.Grochulski, P.Coulombe, R.Storer, A.C.Mort, J.S.

(1996) Structure 4: 405-416

  • DOI: https://doi.org/10.1016/s0969-2126(96)00046-9
  • Primary Citation of Related Structures:  
    1MIR

  • PubMed Abstract: 

    Cysteine proteases of the papain superfamily are synthesized as inactive precursors with a 60-110 residue N-terminal prosegment. The propeptides are potent inhibitors of their parent proteases. Although the proregion binding mode has been elucidated for all other protease classes, that of the cysteine proteases remained elusive.


  • Organizational Affiliation

    Biotechnology Research Institute, National Research Council of Canada, Montreal, Quebec, Canada.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PROCATHEPSIN B
A, B
322Rattus norvegicusMutation(s): 3 
EC: 3.4.22.1
UniProt
Find proteins for P00787 (Rattus norvegicus)
Explore P00787 
Go to UniProtKB:  P00787
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP00787
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.80 Å
  • R-Value Free: 0.270 
  • R-Value Work: 0.220 
  • R-Value Observed: 0.220 
  • Space Group: P 31 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 99.6α = 90
b = 99.6β = 90
c = 141.4γ = 120
Software Package:
Software NamePurpose
R-AXISdata collection
X-PLORmodel building
X-PLORrefinement
R-AXISdata reduction
X-PLORphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1997-01-11
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2020-02-12
    Changes: Advisory, Database references, Derived calculations, Other
  • Version 1.4: 2021-11-03
    Changes: Advisory, Database references