2F8A

Crystal structure of the selenocysteine to glycine mutant of human glutathione peroxidase 1


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.50 Å
  • R-Value Free: 0.156 
  • R-Value Work: 0.138 
  • R-Value Observed: 0.138 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Crystal structure of the selenocysteine to glycine mutant of human glutathione peroxidase 1

Kavanagh, K.L.Johansson, C.Smee, C.Gileadi, O.von Delft, F.Oppermann, U.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Glutathione peroxidase 1
A, B
208Homo sapiensMutation(s): 0 
Gene Names: GPX1
EC: 1.11.1.9
UniProt & NIH Common Fund Data Resources
Find proteins for P07203 (Homo sapiens)
Explore P07203 
Go to UniProtKB:  P07203
PHAROS:  P07203
GTEx:  ENSG00000233276 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP07203
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.50 Å
  • R-Value Free: 0.156 
  • R-Value Work: 0.138 
  • R-Value Observed: 0.138 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 127.592α = 90
b = 59.376β = 119.41
c = 81.132γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
MOSFLMdata reduction
CCP4data scaling
PHASERphasing

Structure Validation

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Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2005-12-13
    Type: Initial release
  • Version 1.1: 2008-05-01
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Advisory, Version format compliance
  • Version 1.3: 2015-04-29
    Changes: Non-polymer description
  • Version 1.4: 2023-08-30
    Changes: Data collection, Database references, Derived calculations, Refinement description