3PYZ | pdb_00003pyz

Crystal structure of bifunctional folylpolyglutamate synthase/dihydrofolate synthase complexed with AMPPNP and Mn ion from Yersinia pestis c092

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.10 Å
  • R-Value Free: 
    0.228 (Depositor), 0.230 (DCC) 
  • R-Value Work: 
    0.176 (Depositor), 0.190 (DCC) 
  • R-Value Observed: 
    0.179 (Depositor) 

Starting Model: experimental
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Ligand Structure Quality Assessment 

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This is version 1.2 of the entry. See complete history. 


Literature

Crystal structure of bifunctional folylpolyglutamate synthase/dihydrofolate synthase complexed with AMPpnp and Mn ion from Yersinia pestis c092

Nocek, B., Makowska-Grzyska, M., Maltseva, N., Anderson, W., Joachimiak, A., Center for Structural Genomics of Infectious Diseases (CSGID)

To be published.

Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Bifunctional folylpolyglutamate synthase/dihydrofolate synthase437Yersinia pestis CO92Mutation(s): 0 
Gene Names: folC, YPN_2178, YP516_2438
EC: 6.3.2.12 (PDB Primary Data), 6.3.2.17 (PDB Primary Data)
UniProt
Find proteins for Q8D0U0 (Yersinia pestis)
Explore Q8D0U0 
Go to UniProtKB:  Q8D0U0
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ8D0U0
Sequence Annotations
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  • Reference Sequence
Small Molecules
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.10 Å
  • R-Value Free:  0.228 (Depositor), 0.230 (DCC) 
  • R-Value Work:  0.176 (Depositor), 0.190 (DCC) 
  • R-Value Observed: 0.179 (Depositor) 
Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 60.627α = 90
b = 77.713β = 90
c = 122.292γ = 90
Software Package:
Software NamePurpose
SBC-Collectdata collection
MOLREPphasing
CCP4model building
REFMACrefinement
HKL-3000data reduction
HKL-3000data scaling
CCP4phasing

Structure Validation

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Ligand Structure Quality Assessment 

Created with Raphaël 2.3.0Worse 01 BetterLigand structure goodness of fit to experimental dataBest fitted ANPClick 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: 2011-01-19
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2023-09-13
    Changes: Data collection, Database references, Derived calculations, Refinement description