5FPW

proCathepsin B S9 from Trypanosoma congolense

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.10 Å
  • R-Value Free: 0.216 
  • R-Value Work: 0.179 
  • R-Value Observed: 0.181 

wwPDB Validation   3D Report Full Report


This is version 2.0 of the entry. See complete history. 


Literature

2.1 Angstrom Crystal Structure of Pro Cathepsin B S9 from Trypanosoma Congolense

Sevajol, M., Biteau, N., Baltz, T., Franzetti, B., Vellieux, F.M.D.

(null) Ph D Thesis 


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PRO CATHEPSIN B S9
A, B, C
321Trypanosoma congolenseMutation(s): 2 
EC: 3.4.22.1
UniProt
Find proteins for B2C331 (Trypanosoma congolense)
Explore B2C331 
Go to UniProtKB:  B2C331
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupB2C331
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.10 Å
  • R-Value Free: 0.216 
  • R-Value Work: 0.179 
  • R-Value Observed: 0.181 
  • Space Group: C 2 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 128.79α = 90
b = 223.22β = 90
c = 102.89γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
XDSdata reduction
XSCALEdata scaling

Structure Validation

View Full Validation Report



View more in-depth experimental data
Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2016-02-17
    Type: Initial release
  • Version 2.0: 2019-03-06
    Changes: Advisory, Atomic model, Data collection, Experimental preparation, Other