6BN2

Crystal structure of Acetyl-CoA acetyltransferase from Elizabethkingia anophelis NUHP1


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.65 Å
  • R-Value Free: 0.156 
  • R-Value Work: 0.138 
  • R-Value Observed: 0.139 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

Crystal structure of Acetyl-CoA acetyltransferase from Elizabethkingia anophelis NUHP1

Abendroth, J.Fox III, D.Lorimer, D.D.Edwards, T.E.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Acetyl-CoA acetyltransferase401Elizabethkingia anophelis NUHP1Mutation(s): 0 
Gene Names: BD94_2261
EC: 2.3.1.9
UniProt
Find proteins for A0A077EEP0 (Elizabethkingia anophelis NUHP1)
Explore A0A077EEP0 
Go to UniProtKB:  A0A077EEP0
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A077EEP0
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.65 Å
  • R-Value Free: 0.156 
  • R-Value Work: 0.138 
  • R-Value Observed: 0.139 
  • Space Group: C 2 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 99.17α = 90
b = 167.42β = 90
c = 72.56γ = 90
Software Package:
Software NamePurpose
XSCALEdata scaling
PHENIXrefinement
PDB_EXTRACTdata extraction
XDSdata reduction
MoRDaphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2018-01-17
    Type: Initial release
  • Version 1.1: 2023-10-04
    Changes: Data collection, Database references, Derived calculations, Refinement description