3OJ7

Crystal structure of a histidine triad family protein from entamoeba histolytica, bound to sulfate


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.40 Å
  • R-Value Free: 0.184 
  • R-Value Work: 0.162 
  • R-Value Observed: 0.163 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Structures of a histidine triad family protein from Entamoeba histolytica bound to sulfate, AMP and GMP.

Lorimer, D.D.Choi, R.Abramov, A.Nakazawa Hewitt, S.Gardberg, A.S.Van Voorhis, W.C.Staker, B.L.Myler, P.J.Edwards, T.E.

(2015) Acta Crystallogr F Struct Biol Commun 71: 572-576

  • DOI: https://doi.org/10.1107/S2053230X1500237X
  • Primary Citation of Related Structures:  
    3OJ7, 3OMF, 3OXK

  • PubMed Abstract: 

    Three structures of the histidine triad family protein from Entamoeba histolytica, the causative agent of amoebic dysentery, were solved at high resolution within the Seattle Structural Genomics Center for Infectious Disease (SSGCID). The structures have sulfate (PDB entry 3oj7), AMP (PDB entry 3omf) or GMP (PDB entry 3oxk) bound in the active site, with sulfate occupying the same space as the α-phosphate of the two nucleotides. The C(α) backbones of the three structures are nearly superimposable, with pairwise r.m.s.d.s ranging from 0.06 to 0.13 Å.


  • Organizational Affiliation

    Seattle Structural Genomics Center for Infectious Disease, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Putative histidine triad family protein117Entamoeba histolytica HM-1:IMSSMutation(s): 0 
Gene Names: EHI_093910
UniProt
Find proteins for C4LYI2 (Entamoeba histolytica (strain ATCC 30459 / HM-1:IMSS / ABRM))
Explore C4LYI2 
Go to UniProtKB:  C4LYI2
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupC4LYI2
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

Unit Cell:
Length ( Å )Angle ( ˚ )
a = 52.89α = 90
b = 61.03β = 90
c = 67.31γ = 90
Software Package:
Software NamePurpose
ADSCdata collection
PHASERphasing
REFMACrefinement
XDSdata reduction
XSCALEdata scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2010-09-08
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2015-05-20
    Changes: Database references
  • Version 1.3: 2023-09-06
    Changes: Data collection, Database references, Derived calculations, Refinement description