3Q1H

Crystal Structure of Dihydrofolate Reductase from Yersinia pestis


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Free: 0.200 
  • R-Value Work: 0.166 
  • R-Value Observed: 0.167 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Crystal Structure of Dihydrofolate Reductase from Yersinia pestis

Maltseva, N.Kim, Y.Makowska-Grzyska, M.Mulligan, R.Papazisi, L.Anderson, W.F.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
Dihydrofolate reductase163Yersinia pestis CO92Mutation(s): 0 
Gene Names: folAy3688YPO0486YP_3693
EC: 1.5.1.3
UniProt
Find proteins for A0A3N4BLI0 (Yersinia pestis)
Explore A0A3N4BLI0 
Go to UniProtKB:  A0A3N4BLI0
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A3N4BLI0
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

Unit Cell:
Length ( Å )Angle ( ˚ )
a = 60.477α = 90
b = 79.152β = 90
c = 64.685γ = 90
Software Package:
Software NamePurpose
SBC-Collectdata collection
HKL-3000data collection
BALBESphasing
PHENIXrefinement
HKL-3000data reduction
HKL-3000data scaling

Structure Validation

View Full Validation Report



Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2011-01-12
    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