3M1X

Crystal structure of a putative endoribonuclease L-PSP from Entamoeba histolytica, rhomobohedral form


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.20 Å
  • R-Value Free: 0.131 
  • R-Value Work: 0.106 
  • R-Value Observed: 0.107 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Crystal structure of a putative endoribonuclease L-PSP from Entamoeba histolytica, rhomobohedral form

Gardberg, A.Abendroth, J.Davies, D.Staker, B.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
putative Endoribonuclease L-PSP148Entamoeba histolytica HM-1:IMSSMutation(s): 0 
Gene Names: EHI_087570
UniProt
Find proteins for C4LXT9 (Entamoeba histolytica (strain ATCC 30459 / HM-1:IMSS / ABRM))
Explore C4LXT9 
Go to UniProtKB:  C4LXT9
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupC4LXT9
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
MHO
Query on MHO
A
L-PEPTIDE LINKINGC5 H11 N O3 SMET
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.20 Å
  • R-Value Free: 0.131 
  • R-Value Work: 0.106 
  • R-Value Observed: 0.107 
  • Space Group: H 3 2
  • Diffraction Data: https://doi.org/10.18430/M33M1X
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 78.546α = 90
b = 78.546β = 90
c = 89.18γ = 120
Software Package:
Software NamePurpose
Blu-Icedata collection
PHASERphasing
REFMACrefinement
XDSdata reduction
SCALAdata scaling

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2010-03-31
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2023-09-06
    Changes: Data collection, Database references, Derived calculations, Refinement description