4E79

Structure of LpxD from Acinetobacter baumannii at 2.66A resolution (P4322 form)


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.66 Å
  • R-Value Free: 0.300 
  • R-Value Work: 0.234 
  • R-Value Observed: 0.237 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Structure determination of LpxD from the lipopolysaccharide-synthesis pathway of Acinetobacter baumannii.

Badger, J.Chie-Leon, B.Logan, C.Sridhar, V.Sankaran, B.Zwart, P.H.Nienaber, V.

(2013) Acta Crystallogr Sect F Struct Biol Cryst Commun 69: 6-9

  • DOI: https://doi.org/10.1107/S1744309112048890
  • Primary Citation of Related Structures:  
    4E75, 4E79

  • PubMed Abstract: 

    Acinetobacter baumannii is a Gram-negative bacterium that is resistant to many currently available antibiotics. The protein LpxD is a component of the biosynthetic pathway for lipopolysaccharides in the outer membrane of this bacterium and is a potential target for new antibacterial agents. This paper describes the structure determination of apo forms of LpxD in space groups P2(1) and P4(3)22. These crystals contained six and three copies of the protein molecule in the asymmetric unit and diffracted to 2.8 and 2.7 Å resolution, respectively. A comparison of the multiple protein copies in the asymmetric units of these crystals reveals a common protein conformation and a conformation in which the relative orientation between the two major domains in the protein is altered.


  • Organizational Affiliation

    Zenobia Therapeutics Inc., 505 Coast Boulevard South, Suite 111, La Jolla, CA 92037, USA. john@zenobiatherapeutics.com


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
UDP-3-O-acylglucosamine N-acyltransferase
A, B, C
357Acinetobacter baumanniiMutation(s): 0 
Gene Names: lpxDABSDF1688
EC: 2.3.1
UniProt
Find proteins for B0VMV2 (Acinetobacter baumannii (strain SDF))
Explore B0VMV2 
Go to UniProtKB:  B0VMV2
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupB0VMV2
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.66 Å
  • R-Value Free: 0.300 
  • R-Value Work: 0.234 
  • R-Value Observed: 0.237 
  • Space Group: P 43 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 64.667α = 90
b = 64.667β = 90
c = 463.814γ = 90
Software Package:
Software NamePurpose
PHASERphasing
REFMACrefinement
HKL-2000data reduction
HKL-2000data scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2013-01-16
    Type: Initial release
  • Version 1.1: 2013-02-20
    Changes: Database references
  • Version 1.2: 2023-09-13
    Changes: Data collection, Database references, Refinement description