4HY3

Crystal structure of a phosphoglycerate oxidoreductase from rhizobium etli


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.80 Å
  • R-Value Free: 0.291 
  • R-Value Work: 0.204 
  • R-Value Observed: 0.208 

wwPDB Validation   3D Report Full Report


This is version 1.0 of the entry. See complete history


Literature

Crystal structure of a phosphoglycerate oxidoreductase from rhizobium etli

Kumaran, D.Almo, S.C.Swaminathan, S.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
phosphoglycerate oxidoreductase
A, B, C, D
365Rhizobium etli CFN 42Mutation(s): 0 
Gene Names: RHE_PB00144
UniProt
Find proteins for Q2K273 (Rhizobium etli (strain CFN 42 / ATCC 51251))
Explore Q2K273 
Go to UniProtKB:  Q2K273
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ2K273
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
MSE
Query on MSE
A, B, C, D
L-PEPTIDE LINKINGC5 H11 N O2 SeMET
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.80 Å
  • R-Value Free: 0.291 
  • R-Value Work: 0.204 
  • R-Value Observed: 0.208 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 61.733α = 90
b = 121.118β = 101.4
c = 106.652γ = 90
Software Package:
Software NamePurpose
CBASSdata collection
SHELXDphasing
SHELXEmodel building
ARP/wARPmodel building
REFMACrefinement
HKL-2000data reduction
HKL-2000data scaling

Structure Validation

View Full Validation Report



Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2012-12-12
    Type: Initial release