4S1V

Crystal structure of phosphoglycerate oxidoreductase from Vibrio Cholerae o395

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.10 Å
  • R-Value Free: 0.243 
  • R-Value Work: 0.202 
  • R-Value Observed: 0.204 

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


Literature

Crystal Structure of Phosphoglycerate Oxidoreductase from Vibrio Cholerae O395

Tarique, K.F., Rehman, S.A.A., Devi, S., Gourinath, S.

To be published.

Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
D-3-phosphoglycerate dehydrogenase-related proteinA [auth D],
B [auth A],
C [auth B],
D [auth C]		332Vibrio cholerae O395Mutation(s): 0 
Gene Names: VC0395_0573, VC395_A0682
EC: 1.1.1.95
UniProt
Find proteins for A0A0H2UKZ7 (Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395))
Explore A0A0H2UKZ7 
Go to UniProtKB:  A0A0H2UKZ7
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A0H2UKZ7
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.10 Å
  • R-Value Free: 0.243 
  • R-Value Work: 0.202 
  • R-Value Observed: 0.204 
  • Space Group: P 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 51.916α = 64.39
b = 83.258β = 81.94
c = 85.986γ = 76.03
Software Package:
Software NamePurpose
MAR345dtbdata collection
PHASERphasing
REFMACrefinement
HKL-2000data reduction
HKL-2000data scaling

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2015-01-28
    Type: Initial release
  • Version 1.1: 2023-09-20
    Changes: Data collection, Database references, Refinement description