1FEB

UNLIGANDED CRITHIDIA FASCICULATA TRYPANOTHIONE REDUCTASE AT 2.0 ANGSTROM RESOLUTION


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Work: 0.202 
  • R-Value Observed: 0.202 

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Ligand Structure Quality Assessment 


This is version 1.3 of the entry. See complete history


Literature

Crithidia Fasciculata Trypanothione Reductase at 1.70 A Resolution

Strickland, C.L.Karplus, P.A.

To be published.

Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
TRYPANOTHIONE REDUCTASE
A, B
490Crithidia fasciculataMutation(s): 0 
Gene Names: TR1
EC: 1.6.4.8 (PDB Primary Data), 1.8.1.12 (UniProt)
UniProt
Find proteins for P39040 (Crithidia fasciculata)
Explore P39040 
Go to UniProtKB:  P39040
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP39040
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Work: 0.202 
  • R-Value Observed: 0.202 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 105.9α = 90
b = 169.6β = 90
c = 60γ = 90
Software Package:
Software NamePurpose
SDMSdata collection
SCALEPACKdata scaling
X-PLORmodel building
X-PLORrefinement
SDMSdata reduction
X-PLORphasing

Structure Validation

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Ligand Structure Quality Assessment 


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: 2024-10-30
    Changes: Data collection, Database references, Derived calculations, Structure summary