7OG3

IRED-88

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.232 
  • R-Value Work: 0.206 
  • R-Value Observed: 0.207 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


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


Literature

Machine-Directed Evolution of an Imine Reductase for Activity and Stereoselectivity

Ma, E.J., Siirola, E., Moore, C., Kummer, A., Stoeckli, M., Faller, M., Bouquet, C., Eggimann, F., Ligibel, M., Huynh, D., Cutler, G., Siegrist, L., Lewis, R.A., Acker, A.C., Freund, E., Koch, E., Vogel, M., Schlingensiepen, H., Oakeley, E.J., Snajdrova, R.

(2021) ACS Catal : 12433-12445


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
NAD(P)-dependent oxidoreductase
A, B
323Streptomyces spectabilisMutation(s): 0 
Gene Names: CP982_37880
UniProt
Find proteins for A0A5P2XKZ4 (Streptomyces spectabilis)
Explore A0A5P2XKZ4 
Go to UniProtKB:  A0A5P2XKZ4
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A5P2XKZ4
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.232 
  • R-Value Work: 0.206 
  • R-Value Observed: 0.207 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 73.856α = 90
b = 75.746β = 90
c = 97.081γ = 90
Software Package:
Software NamePurpose
BUSTERrefinement
XDSdata reduction
XSCALEdata scaling
PHASERphasing

Structure Validation

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Ligand Structure Quality Assessment 


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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2021-10-06
    Type: Initial release
  • Version 1.1: 2024-01-31
    Changes: Data collection, Refinement description