6V45

Crystal structure of a Probable carnitine operon oxidoreductase caia from Brucella melitensis


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.60 Å
  • R-Value Free: 0.235 
  • R-Value Work: 0.199 
  • R-Value Observed: 0.202 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

Crystal structure of a Probable carnitine operon oxidoreductase caia from Brucella melitensis

Abendroth, J.Lorimer, D.D.Horanyi, P.S.Edwards, T.E.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Probable carnitine operon oxidoreductase caia209Brucella melitensis bv. 1 str. 16MMutation(s): 0 
Gene Names: BMEI0848
EC: 1.3.99
UniProt
Find proteins for Q8YHF3 (Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094))
Explore Q8YHF3 
Go to UniProtKB:  Q8YHF3
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ8YHF3
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.60 Å
  • R-Value Free: 0.235 
  • R-Value Work: 0.199 
  • R-Value Observed: 0.202 
  • Space Group: P 2 3
  • Diffraction Data: https://doi.org/10.18430/m36v45
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 96.06α = 90
b = 96.06β = 90
c = 96.06γ = 90
Software Package:
Software NamePurpose
XDSdata reduction
XSCALEdata scaling
PHENIXrefinement
PDB_EXTRACTdata extraction
MR-Rosettaphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2019-12-11
    Type: Initial release
  • Version 1.1: 2024-03-06
    Changes: Data collection, Database references