2A0M

Arginase superfamily protein from Trypanosoma cruzi


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.60 Å
  • R-Value Free: 0.195 
  • R-Value Work: 0.168 

wwPDB Validation   3D Report Full Report


This is version 1.6 of the entry. See complete history


Literature

Structural genomics of pathogenic protozoa: an overview.

Fan, E.Baker, D.Fields, S.Gelb, M.H.Buckner, F.S.Van Voorhis, W.C.Phizicky, E.Dumont, M.Mehlin, C.Grayhack, E.Sullivan, M.Verlinde, C.Detitta, G.Meldrum, D.R.Merritt, E.A.Earnest, T.Soltis, M.Zucker, F.Myler, P.J.Schoenfeld, L.Kim, D.Worthey, L.Lacount, D.Vignali, M.Li, J.Mondal, S.Massey, A.Carroll, B.Gulde, S.Luft, J.Desoto, L.Holl, M.Caruthers, J.Bosch, J.Robien, M.Arakaki, T.Holmes, M.Le Trong, I.Hol, W.G.

(2008) Methods Mol Biol 426: 497-513

  • DOI: https://doi.org/10.1007/978-1-60327-058-8_33
  • Primary Citation of Related Structures:  
    2A0M

  • PubMed Abstract: 

    The Structural Genomics of Pathogenic Protozoa (SGPP) Consortium aimed to determine crystal structures of proteins from trypanosomatid and malaria parasites in a high throughput manner. The pipeline of target selection, protein production, crystallization, and structure determination, is sketched. Special emphasis is given to a number of technology developments including domain prediction, the use of "co-crystallants," and capillary crystallization. "Fragment cocktail crystallography" for medical structural genomics is also described.


  • Organizational Affiliation

    Department of Biochemistry, University of Washington, Seattle, WA, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
ARGINASE SUPERFAMILY PROTEIN316Trypanosoma cruziMutation(s): 0 
Gene Names: Tc00.1047053507963.20
EC: 3.5.3.8
UniProt
Find proteins for Q4DSA0 (Trypanosoma cruzi (strain CL Brener))
Explore Q4DSA0 
Go to UniProtKB:  Q4DSA0
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ4DSA0
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
CL
Query on CL

Download Ideal Coordinates CCD File 
B [auth A]CHLORIDE ION
Cl
VEXZGXHMUGYJMC-UHFFFAOYSA-M
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.60 Å
  • R-Value Free: 0.195 
  • R-Value Work: 0.168 
  • Space Group: H 3
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 128.875α = 90
b = 128.875β = 90
c = 42.671γ = 120
Software Package:
Software NamePurpose
REFMACrefinement
DENZOdata reduction
SCALEPACKdata scaling
PDB_EXTRACTdata extraction
MOLREPphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2005-07-05
    Type: Initial release
  • Version 1.1: 2008-04-30
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Derived calculations, Version format compliance
  • Version 1.3: 2013-10-16
    Changes: Database references
  • Version 1.4: 2017-10-11
    Changes: Advisory, Refinement description
  • Version 1.5: 2024-02-14
    Changes: Advisory, Data collection, Database references, Derived calculations
  • Version 1.6: 2024-04-03
    Changes: Refinement description