1CI0

PNP OXIDASE FROM SACCHAROMYCES CEREVISIAE

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.70 Å
  • R-Value Free: 0.274 
  • R-Value Work: 0.225 
  • R-Value Observed: 0.230 

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Ligand Structure Quality Assessment 


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


Literature

The Structure of PNP Oxidase from S. Cerevisiae

Shi, W., Ostrov, D.A., Gerchman, S.E., Graziano, V., Kycia, H., Studier, B., Almo, S.C.

To be published.

Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEIN (PNP OXIDASE)
A, B
228Saccharomyces cerevisiaeMutation(s): 0 
EC: 1.4.3.5
UniProt
Find proteins for P38075 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Explore P38075 
Go to UniProtKB:  P38075
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP38075
Sequence Annotations
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  • Reference Sequence
Small Molecules
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.70 Å
  • R-Value Free: 0.274 
  • R-Value Work: 0.225 
  • R-Value Observed: 0.230 
  • Space Group: P 32 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 74.97α = 90
b = 74.97β = 90
c = 157.14γ = 120
Software Package:
Software NamePurpose
X-PLORrefinement
SCALEPACKdata scaling

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: 1999-08-25
    Type: Initial release
  • Version 1.1: 2008-04-26
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2021-02-03
    Changes: Derived calculations, Structure summary
  • Version 1.4: 2023-12-27
    Changes: Data collection, Database references