4HWG

Structure of UDP-N-acetylglucosamine 2-epimerase from Rickettsia bellii


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.182 
  • R-Value Work: 0.148 
  • R-Value Observed: 0.150 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

Structure of UDP-N-acetylglucosamine 2-epimerase from Rickettsia bellii

Seattle Structural Genomics Center for Infectious Disease (SSGCID)Abendroth, J.Sankaran, B.Davies, D.R.Edwards, T.E.Staker, B.L.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
UDP-N-acetylglucosamine 2-epimerase385Rickettsia bellii RML369-CMutation(s): 0 
Gene Names: RBE_0708rffE
EC: 5.1.3.14
UniProt
Find proteins for Q1RIM5 (Rickettsia bellii (strain RML369-C))
Explore Q1RIM5 
Go to UniProtKB:  Q1RIM5
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ1RIM5
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
PO4
Query on PO4

Download Ideal Coordinates CCD File 
B [auth A]PHOSPHATE ION
O4 P
NBIIXXVUZAFLBC-UHFFFAOYSA-K
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.182 
  • R-Value Work: 0.148 
  • R-Value Observed: 0.150 
  • Space Group: H 3 2
  • Diffraction Data: https://doi.org/10.18430/M34HWG
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 146.71α = 90
b = 146.71β = 90
c = 106.25γ = 120
Software Package:
Software NamePurpose
XSCALEdata scaling
PHASERphasing
REFMACrefinement
PDB_EXTRACTdata extraction
BOSdata collection
XDSdata reduction

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2012-11-28
    Type: Initial release
  • Version 1.1: 2023-09-20
    Changes: Data collection, Database references, Derived calculations, Refinement description