3N72

Crystal Structure of Aha-1 from plasmodium falciparum, PFC0270w

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.77 Å
  • R-Value Free: 0.247 
  • R-Value Work: 0.188 
  • R-Value Observed: 0.191 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history. 


Literature

Crystal Structure of Aha-1 from plasmodium falciparum, PFC0270w

Wernimont, A.K., Dong, A., Hutchinson, A., Sullivan, H., Mackenzie, F., Kozieradzki, I., Cossar, D., Bochkarev, A., Arrowsmith, C.H., Edwards, A.M., Bountra, C., Weigelt, J., Hui, R., Pizarro, J.C., Hills, T.

To be published.

Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
putative activator of HSP90
A, B
164Plasmodium falciparumMutation(s): 0 
Gene Names: PFC0270w
UniProt
Find proteins for Q689C6 (Plasmodium falciparum)
Explore Q689C6 
Go to UniProtKB:  Q689C6
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ689C6
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
SCN
Query on SCN
Download Ideal Coordinates CCD File 
C [auth B]THIOCYANATE ION
C N S
ZMZDMBWJUHKJPS-UHFFFAOYSA-M
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.77 Å
  • R-Value Free: 0.247 
  • R-Value Work: 0.188 
  • R-Value Observed: 0.191 
  • Space Group: P 31
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 63.709α = 90
b = 63.709β = 90
c = 61.722γ = 120
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
SHELXphasing
REFMACrefinement
PDB_EXTRACTdata extraction
SHELXDphasing

Structure Validation

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View more in-depth experimental data
Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2010-07-21
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2017-11-08
    Changes: Refinement description
  • Version 1.3: 2024-02-21
    Changes: Data collection, Database references, Derived calculations