5TCV

ACC oxidase complex with substrate 1-aminocyclopropane-1-carboxylic acid


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.60 Å
  • R-Value Free: 0.291 
  • R-Value Work: 0.232 
  • R-Value Observed: 0.235 

Starting Model: experimental
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wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

ACC oxidase complex with substrate 1-aminocyclopropane-1-carboxylic acid

Gunawardana, D.M.Arabshahi, J.Yosaatmadja, Y.Reynisson, J.Squire, C.J.Leung, I.K.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
1-aminocyclopropane-1-carboxylate oxidase 1319Petunia x hybridaMutation(s): 0 
Gene Names: ACO1
EC: 1.14.17.4
UniProt
Find proteins for Q08506 (Petunia hybrida)
Explore Q08506 
Go to UniProtKB:  Q08506
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ08506
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.60 Å
  • R-Value Free: 0.291 
  • R-Value Work: 0.232 
  • R-Value Observed: 0.235 
  • Space Group: I 2 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 71.361α = 90
b = 107.14β = 90
c = 108.019γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2017-09-20
    Type: Initial release
  • Version 1.1: 2023-10-04
    Changes: Data collection, Database references, Derived calculations, Refinement description