3LX3 | pdb_00003lx3

Plasmodium vivax 6-pyruvoyltetrahydropterin synthase (PTPS) in complex with xanthopterin

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.55 Å
  • R-Value Free: 
    0.167 (Depositor), 0.180 (DCC) 
  • R-Value Work: 
    0.149 (Depositor), 0.160 (DCC) 
  • R-Value Observed: 
    0.150 (Depositor) 

Starting Model: experimental
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wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 

Created with Raphaël 2.3.0Worse 01 BetterLigand structure goodness of fit to experimental dataBest fitted XTNClick on this verticalbar to view details

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


Literature

Structural analysis of the dual-functional 6-pyruvoyltetrahydropterin synthase from Malaria parasites.

Larson, E.T., Bosch, J., Kim, J.E., Mueller, N., Verlinde, C.L.M.J., Van Voorhis, W.C., Buckner, F.S., Fan, E., Hol, W.G.J., Merritt, E.A.

To be published.

Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
6-pyruvoyl tetrahydrobiopterin synthase180Plasmodium vivaxMutation(s): 0 
Gene Names: PVX_114505
EC: 4.2.3.12
UniProt
Find proteins for A5K2B2 (Plasmodium vivax (strain Salvador I))
Explore A5K2B2 
Go to UniProtKB:  A5K2B2
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA5K2B2
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.55 Å
  • R-Value Free:  0.167 (Depositor), 0.180 (DCC) 
  • R-Value Work:  0.149 (Depositor), 0.160 (DCC) 
  • R-Value Observed: 0.150 (Depositor) 
Space Group: H 3 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 131.358α = 90
b = 131.358β = 90
c = 73.577γ = 120
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
MOLREPphasing
REFMACrefinement
PDB_EXTRACTdata extraction
Blu-Icedata collection
HKL-2000data reduction
HKL-2000data scaling

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 

Created with Raphaël 2.3.0Worse 01 BetterLigand structure goodness of fit to experimental dataBest fitted XTNClick on this verticalbar to view details

View more in-depth experimental data
Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2010-03-09
    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: 2023-09-06
    Changes: Data collection, Database references, Derived calculations, Refinement description