3ER0

Crystal structure of the full length eIF5A from Saccharomyces cerevisiae


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.35 Å
  • R-Value Free: 0.448 
  • R-Value Work: 0.386 
  • R-Value Observed: 0.392 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Crystal structure of the full length eIF5A from Saccharomyces cerevisiae

Sanches, M.Dias, C.A.O.Aponi, L.H.Valentini, S.R.Guimaraes, B.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Eukaryotic translation initiation factor 5A-2
A, B
167Saccharomyces cerevisiaeMutation(s): 0 
Gene Names: HYP2TIF51AYEL034WSYGP-ORF21
UniProt
Find proteins for P23301 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Explore P23301 
Go to UniProtKB:  P23301
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP23301
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.35 Å
  • R-Value Free: 0.448 
  • R-Value Work: 0.386 
  • R-Value Observed: 0.392 
  • Space Group: P 65 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 59.664α = 90
b = 59.664β = 90
c = 339.79γ = 120
Software Package:
Software NamePurpose
MAR345dtbdata collection
PHASERphasing
REFMACrefinement
MOSFLMdata reduction
SCALAdata scaling

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2008-12-02
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2023-09-06
    Changes: Data collection, Database references, Refinement description