1F2E

STRUCTURE OF SPHINGOMONAD, GLUTATHIONE S-TRANSFERASE COMPLEXED WITH GLUTATHIONE


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.236 
  • R-Value Work: 0.198 
  • R-Value Observed: 0.198 

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Ligand Structure Quality Assessment 


This is version 1.3 of the entry. See complete history


Literature

Properties of a Sphingomonad and Marine Bacterium Beta-Class Glutathione S-Transferases and Crystal Structure of the Former Complex with Glutathione

Nishio, T.Watanabe, T.Patel, A.Wang, Y.Lau, P.C.K.Grochulski, P.Li, Y.Cygler, M.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
GLUTATHIONE S-TRANSFERASE
A, B, C, D
201Sphingomonas paucimobilisMutation(s): 0 
EC: 2.5.1.18
UniProt
Find proteins for O33705 (Sphingomonas paucimobilis)
Explore O33705 
Go to UniProtKB:  O33705
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO33705
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.236 
  • R-Value Work: 0.198 
  • R-Value Observed: 0.198 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 97.505α = 90
b = 44.792β = 98.6
c = 116.459γ = 90
Software Package:
Software NamePurpose
AMoREphasing
CNSrefinement
DENZOdata reduction
SCALEPACKdata scaling

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2000-06-21
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2011-12-21
    Changes: Non-polymer description