5EID

AKR2A ankyrin repeat domain

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.235 
  • R-Value Work: 0.187 
  • R-Value Observed: 0.190 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history. 


Literature

structure of AKR2A ankyrin repeat domain at 2.0 angstroms resolution

Pu, H., Li, H.

To be published.

Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Ankyrin repeat domain-containing protein 2168Arabidopsis thalianaMutation(s): 0 
Gene Names: AKR2, AFT, At4g35450, F15J1.20
UniProt
Find proteins for Q9SAR5 (Arabidopsis thaliana)
Explore Q9SAR5 
Go to UniProtKB:  Q9SAR5
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9SAR5
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.235 
  • R-Value Work: 0.187 
  • R-Value Observed: 0.190 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 124.141α = 90
b = 39.193β = 96.29
c = 28.499γ = 90
Software Package:
Software NamePurpose
HKL-2000data collection
HKL-2000data scaling
PHASERphasing
PHENIXrefinement
PDB_EXTRACTdata extraction
PHENIXmodel building

Structure Validation

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View more in-depth experimental data
Entry History & Funding Information

Deposition Data

  • Released Date: 2016-11-02 
    • Deposition Author(s): Pu, H., Li, H.
Funding OrganizationLocationGrant Number
National Natural Science FoundationChina31300634

Revision History  (Full details and data files)

  • Version 1.0: 2016-11-02
    Type: Initial release
  • Version 1.1: 2023-11-08
    Changes: Data collection, Database references, Derived calculations, Refinement description