9FOA | pdb_00009foa

Artificial photoenzyme with anthraquinone cofactor and wild type streptavidin


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.36 Å
  • R-Value Free: 
    0.182 (Depositor), 0.182 (DCC) 
  • R-Value Work: 
    0.153 (Depositor), 0.153 (DCC) 
  • R-Value Observed: 
    0.155 (Depositor) 

Starting Model: experimental
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This is version 1.1 of the entry. See complete history


Literature

Artificial Metalloenzymes with Two Catalytic Cofactors for Tandem Abiotic Transformations.

Wang, W.Tachibana, R.Zhang, K.Lau, K.Pojer, F.Ward, T.R.Hu, X.

(2025) Angew Chem Int Ed Engl 64: e202422783-e202422783

  • DOI: https://doi.org/10.1002/anie.202422783
  • Primary Citation of Related Structures:  
    9FFJ, 9FNR, 9FOA

  • PubMed Abstract: 

    Artificial metalloenzymes (ArMs) enable the integration of abiotic cofactors within a native protein scaffold, allowing for non-natural catalytic activities. Previous ArMs, however, have primarily relied on single cofactor systems, limiting them to only one catalytic function. Here we present an approach to construct ArMs embedding two catalytic cofactors based on the biotin-streptavidin technology. By incorporating multiple catalytic cofactors into the four binding sites of streptavidin, we engineered programmable ArMs for tandem abiotic transformations including an enantioselective formal C-H hydroxylation and a photooxidation-Michael addition. This work thus outlines a promising strategy for the development of ArMs embedding multiple cofactors.


  • Organizational Affiliation

    EPFL: Ecole Polytechnique Federale de Lausanne, chemistry, SWITZERLAND.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
StreptavidinA [auth D]159Streptomyces avidiniiMutation(s): 0 
UniProt
Find proteins for P22629 (Streptomyces avidinii)
Explore P22629 
Go to UniProtKB:  P22629
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP22629
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.36 Å
  • R-Value Free:  0.182 (Depositor), 0.182 (DCC) 
  • R-Value Work:  0.153 (Depositor), 0.153 (DCC) 
  • R-Value Observed: 0.155 (Depositor) 
Space Group: I 41 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 57.49α = 90
b = 57.49β = 90
c = 183.03γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
XDSdata reduction
XSCALEdata scaling
PHASERphasing

Structure Validation

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Ligand Structure Quality Assessment 


Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Swiss National Science FoundationSwitzerland--

Revision History  (Full details and data files)

  • Version 1.0: 2025-01-15
    Type: Initial release
  • Version 1.1: 2025-02-26
    Changes: Database references