6GRL

Structure of imine reductase (apo form) at 1.6 A resolution from Saccharomonospora xinjiangensis


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.60 Å
  • R-Value Free: 0.216 
  • R-Value Work: 0.193 
  • R-Value Observed: 0.194 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

Structure of imine reductase (apo form) at 1.6 A resolution from Saccharomonospora xinjiangensis

Hasan, M.Gand, M.Logan, D.T.Hoehne, M.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Beta-hydroxyacid dehydrogenase, 3-hydroxyisobutyrate dehydrogenase305Saccharomonospora xinjiangensis XJ-54Mutation(s): 0 
Gene Names: SacxiDRAFT_0617
UniProt
Find proteins for I0UYD6 (Saccharomonospora xinjiangensis XJ-54)
Explore I0UYD6 
Go to UniProtKB:  I0UYD6
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupI0UYD6
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.60 Å
  • R-Value Free: 0.216 
  • R-Value Work: 0.193 
  • R-Value Observed: 0.194 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 141.184α = 90
b = 35.774β = 91.94
c = 53.05γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
XDSdata reduction
XDSdata scaling
PHASERphasing

Structure Validation

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Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
European UnionGermanyECOST-STSM-CM1303-040515-058745

Revision History  (Full details and data files)

  • Version 1.0: 2019-06-19
    Type: Initial release
  • Version 1.1: 2024-01-17
    Changes: Data collection, Database references, Refinement description