1GP1

THE REFINED STRUCTURE OF THE SELENOENZYME GLUTATHIONE PEROXIDASE AT 0.2-NM RESOLUTION


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Work: 0.171 

wwPDB Validation   3D Report Full Report


This is version 3.0 of the entry. See complete history


Literature

The refined structure of the selenoenzyme glutathione peroxidase at 0.2-nm resolution.

Epp, O.Ladenstein, R.Wendel, A.

(1983) Eur J Biochem 133: 51-69


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
GLUTATHIONE PEROXIDASE
A, B
198Bos taurusMutation(s): 0 
EC: 1.11.1.9 (PDB Primary Data), 1.11.1.12 (UniProt)
UniProt
Find proteins for P00435 (Bos taurus)
Explore P00435 
Go to UniProtKB:  P00435
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP00435
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
SE7
Query on SE7
A, B
L-PEPTIDE LINKINGC3 H7 N O4 SeSEC
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Work: 0.171 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 90.4α = 90
b = 109.5β = 99
c = 58.2γ = 90
Software Package:
Software NamePurpose
EREFrefinement

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1985-11-08
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Advisory, Version format compliance
  • Version 1.3: 2013-12-25
    Changes: Non-polymer description
  • Version 2.0: 2017-11-29
    Changes: Advisory, Derived calculations, Other, Polymer sequence
  • Version 3.0: 2023-07-26
    Type: Remediation
    Changes: Advisory, Atomic model, Data collection, Database references, Derived calculations, Other, Refinement description