1CI0 | pdb_00001ci0

PNP OXIDASE FROM SACCHAROMYCES CEREVISIAE


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.70 Å
  • R-Value Free: 
    0.274 (Depositor) 
  • R-Value Work: 
    0.225 (Depositor), 0.234 (DCC) 
  • R-Value Observed: 
    0.230 (Depositor) 

wwPDB Validation 3D Report Full Report

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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.

Macromolecule Content 

  • Total Structure Weight: 54.81 kDa 
  • Atom Count: 3,441 
  • Modeled Residue Count: 409 
  • Deposited Residue Count: 456 
  • Unique protein chains: 1

Macromolecules

Find similar proteins by:|  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

Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.70 Å
  • R-Value Free:  0.274 (Depositor) 
  • R-Value Work:  0.225 (Depositor), 0.234 (DCC) 
  • R-Value Observed: 0.230 (Depositor) 
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 


Entry History 

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