4HOJ

Crystal structure of glutathione transferase homolog from Neisseria Gonorrhoeae, target EFI-501841, with bound glutathione


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.40 Å
  • R-Value Free: 0.207 
  • R-Value Work: 0.176 
  • R-Value Observed: 0.177 

Starting Model: experimental
View more details

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.1 of the entry. See complete history


Literature

Crystal structure of glutathione transferase homolog from Neisseria Gonorrhoeae, target EFI-501841, with bound glutathione

Vetting, M.W.Toro, R.Bhosle, R.Al Obaidi, N.F.Morisco, L.L.Wasserman, S.R.Sojitra, S.Washington, E.Scott Glenn, A.Chowdhury, S.Evans, B.Hammonds, J.Hillerich, B.Love, J.Seidel, R.D.Imker, H.J.Armstrong, R.N.Gerlt, J.A.Almo, S.C.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
RegF protein210Neisseria gonorrhoeaeMutation(s): 0 
Gene Names: regF
UniProt
Find proteins for O33374 (Neisseria gonorrhoeae)
Explore O33374 
Go to UniProtKB:  O33374
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO33374
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.40 Å
  • R-Value Free: 0.207 
  • R-Value Work: 0.176 
  • R-Value Observed: 0.177 
  • Space Group: P 31 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 49.876α = 90
b = 49.876β = 90
c = 160.236γ = 120
Software Package:
Software NamePurpose
SCALAdata scaling
PHENIXrefinement
PDB_EXTRACTdata extraction
MOSFLMdata reduction
AMoREphasing

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2012-11-07
    Type: Initial release
  • Version 1.1: 2023-09-20
    Changes: Data collection, Database references, Derived calculations, Refinement description