2PGD

THE STRUCTURE OF 6-PHOSPHOGLUCONATE DEHYDROGENASE REFINED AT 2 ANGSTROMS RESOLUTION

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Work: 0.198 
  • R-Value Observed: 0.198 

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This is version 1.4 of the entry. See complete history. 


Literature

The structure of 6-phosphogluconate dehydrogenase refined at 2.5 A resolution.

Adams, M.J., Gover, S., Leaback, R., Phillips, C., Somers, D.O.

(1991) Acta Crystallogr B 47: 817-820

  • DOI: https://doi.org/10.1107/s0108768191010315
  • Primary Citation of Related Structures:  
    2PGD

  • PubMed Abstract: 

    The three-dimensional structure of ovine 6-phosphogluconate dehydrogenase, refined at 2.5 A resolution with a residual for all data of 18.5%, is reported. This model, based on improved diffraction data and a corrected sequence, supersedes that reported earlier. Each subunit of the dimer has three domains: a beta-alpha-beta domain binds NADP; an all alpha domain provides much of the dimer interface; the C-terminal tail burrows into the second subunit.

    • Organizational Affiliation: 

    Laboratory of Molecular Biophysics, Oxford University, England.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
6-PHOSPHOGLUCONATE DEHYDROGENASE482Ovis ariesMutation(s): 0 
EC: 1.1.1.44
UniProt
Find proteins for P00349 (Ovis aries)
Explore P00349 
Go to UniProtKB:  P00349
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP00349
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Work: 0.198 
  • R-Value Observed: 0.198 
  • Space Group: C 2 2 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 72.74α = 90
b = 148.4β = 90
c = 102.35γ = 90
Software Package:
Software NamePurpose
X-PLORmodel building
X-PLORrefinement
X-PLORphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1995-02-27
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Derived calculations, Version format compliance
  • Version 1.3: 2017-11-29
    Changes: Derived calculations, Other
  • Version 1.4: 2024-02-21
    Changes: Data collection, Database references, Derived calculations