8IN2

4,5-DOPA-extradiol-dioxygenase from Beta vulgaris


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.08 Å
  • R-Value Free: 0.220 
  • R-Value Work: 0.167 
  • R-Value Observed: 0.172 

wwPDB Validation   3D Report Full Report


This is version 1.0 of the entry. See complete history


Literature

Crystal structure of the 4,5-DOPA-extradiol-dioxygenase from Beta vulgaris

Chiang, C.C.Hsu, C.H.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
4,5-DOPA dioxygenase extradiol
A, B
276Beta vulgarisMutation(s): 0 
Gene Names: DODA
EC: 1.13.11.29
UniProt
Find proteins for Q70FG7 (Beta vulgaris)
Explore Q70FG7 
Go to UniProtKB:  Q70FG7
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ70FG7
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.08 Å
  • R-Value Free: 0.220 
  • R-Value Work: 0.167 
  • R-Value Observed: 0.172 
  • Space Group: P 31 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 95.873α = 90
b = 95.873β = 90
c = 124.908γ = 120
Software Package:
Software NamePurpose
PHENIXrefinement
HKL-2000data reduction
HKL-2000data scaling
PHASERphasing

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Ministry of Science and Technology (MoST, Taiwan)Taiwan111-2113-M-002-015-MY3
Ministry of Science and Technology (MoST, Taiwan)Taiwan111-2311-B-002-008-MY3

Revision History  (Full details and data files)

  • Version 1.0: 2024-04-24
    Type: Initial release