6C46

Crystal structure of dTDP-4-dehydrorhamnose 3,5-epimerase from Elizabethkingia anophelis NUHP1


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.95 Å
  • R-Value Free: 0.203 
  • R-Value Work: 0.160 
  • R-Value Observed: 0.161 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

Crystal structure of dTDP-4-dehydrorhamnose 3,5-epimerase from Elizabethkingia anophelis NUHP1

Abendroth, J.Delker, S.L.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
dTDP-4-dehydrorhamnose 3,5-epimerase
A, B, C, D, E
189Elizabethkingia anophelis NUHP1Mutation(s): 0 
Gene Names: BD94_3275
EC: 5.1.3.13
UniProt
Find proteins for A0A077ENB9 (Elizabethkingia anophelis NUHP1)
Explore A0A077ENB9 
Go to UniProtKB:  A0A077ENB9
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A077ENB9
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

Unit Cell:
Length ( Å )Angle ( ˚ )
a = 139.34α = 90
b = 62.24β = 105.02
c = 131.02γ = 90
Software Package:
Software NamePurpose
XDSdata reduction
XSCALEdata scaling
PHENIXrefinement
PDB_EXTRACTdata extraction
MoRDaphasing
Cootmodel building
PDB_EXTRACTdata extraction

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2018-02-14
    Type: Initial release
  • Version 1.1: 2023-10-04
    Changes: Data collection, Database references, Derived calculations, Refinement description