3AJA

Crystal Structure of MSMEG_6394


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.90 Å
  • R-Value Free: 0.250 
  • R-Value Work: 0.213 
  • R-Value Observed: 0.215 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

Functional characterisation of a lipase essential for mycobacterial viability

Crellin, P.K.Vivian, J.P.Scoble, J.Chow, F.M.West, N.P.Brammananth, R.Proellocks, N.I.Shahine, A.Le Nours, J.Wilce, M.C.J.Britton, W.J.Coppel, R.L.Rossjohn, J.Beddoe, T.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Putative uncharacterized protein
A, B
302Mycolicibacterium smegmatis MC2 155Mutation(s): 0 
Gene Names: MSMEG_6394
Membrane Entity: Yes 
UniProt
Find proteins for A0R619 (Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155))
Explore A0R619 
Go to UniProtKB:  A0R619
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0R619
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.90 Å
  • R-Value Free: 0.250 
  • R-Value Work: 0.213 
  • R-Value Observed: 0.215 
  • Space Group: I 41 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 130.434α = 90
b = 130.434β = 90
c = 209.533γ = 90
Software Package:
Software NamePurpose
CrystalCleardata collection
SOLVEphasing
REFMACrefinement
MOSFLMdata reduction
SCALAdata scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2010-08-11
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance