3O0H

Crystal structure of glutathione reductase from Bartonella henselae


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.209 
  • R-Value Work: 0.164 
  • R-Value Observed: 0.167 

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Ligand Structure Quality Assessment 


This is version 1.2 of the entry. See complete history


Literature

Crystal structure of glutathione reductase from Bartonella henselae

Seattle Structural Genomics Center for Infectious Disease (SSGCID)Abendroth, J.Edwards, T.E.Staker, B.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Glutathione reductase
A, B
484Bartonella henselae str. Houston-1Mutation(s): 0 
Gene Names: gorBH06430
EC: 1.8.1.7
UniProt
Find proteins for A0A0H3LWY9 (Bartonella henselae (strain ATCC 49882 / DSM 28221 / CCUG 30454 / Houston 1))
Explore A0A0H3LWY9 
Go to UniProtKB:  A0A0H3LWY9
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A0H3LWY9
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

Unit Cell:
Length ( Å )Angle ( ˚ )
a = 84.47α = 90
b = 64.65β = 107.24
c = 90.19γ = 90
Software Package:
Software NamePurpose
StructureStudiodata collection
PHASERphasing
REFMACrefinement
XDSdata reduction
XSCALEdata scaling

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2010-08-18
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2023-09-06
    Changes: Data collection, Database references, Derived calculations, Refinement description