1QMV

thioredoxin peroxidase B from red blood cells

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Free: 0.256 
  • R-Value Work: 0.192 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history. 


Literature

Crystal Structure of Decameric 2-Cys Peroxiredoxin from Human Erythrocytes at 1.7 A Resolution.

Schroder, E., Littlechild, J.A., Lebedev, A.A., Errington, N., Vagin, A.A., Isupov, M.N.

(2000) Structure 8: 605

  • DOI: https://doi.org/10.1016/s0969-2126(00)00147-7
  • Primary Citation of Related Structures:  
    1QMV

  • PubMed Abstract: 

    The peroxiredoxins (Prxs) are an emerging family of multifunctional enzymes that exhibit peroxidase activity in vitro, and in vivo participate in a range of cellular processes known to be sensitive to reactive oxygen species. Thioredoxin peroxidase B (TPx-B), a 2-Cys type II Prx from erythrocytes, promotes potassium efflux and down-regulates apoptosis and the recruitment of monocytes by endothelial tissue.

    • Organizational Affiliation: 

    Schools of Chemistry and Biological Sciences, University of Exeter, Exeter, EX4 4QD, UK. eschrode@ex.ac.uk


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PEROXIREDOXIN-2
A, B, C, D, E
A, B, C, D, E, F, G, H, I, J
197Homo sapiensMutation(s): 0 
EC: 1.11.1.15
UniProt & NIH Common Fund Data Resources
Find proteins for P32119 (Homo sapiens)
Explore P32119 
Go to UniProtKB:  P32119
PHAROS:  P32119
GTEx:  ENSG00000167815 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP32119
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Modified Residues  2 Unique
IDChains TypeFormula2D DiagramParent
CSD
Query on CSD
A, B, C, D, E
A, B, C, D, E, F, G, H, I, J
L-PEPTIDE LINKINGC3 H7 N O4 SCYS
NCB
Query on NCB
A, B, C, D, E
A, B, C, D, E, F, G, H, I, J
L-PEPTIDE LINKINGC4 H8 N2 O3ALA
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Free: 0.256 
  • R-Value Work: 0.192 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 88.88α = 90
b = 107.03β = 110.87
c = 119.5γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
AMoREphasing
MOLREPphasing
REFMACrefinement

Structure Validation

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View more in-depth experimental data
Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2000-07-28
    Type: Initial release
  • Version 1.1: 2013-01-30
    Changes: Advisory, Database references, Derived calculations, Non-polymer description, Other, Structure summary, Version format compliance
  • Version 1.2: 2014-10-22
    Changes: Database references, Other
  • Version 1.3: 2019-07-24
    Changes: Data collection, Derived calculations
  • Version 1.4: 2023-12-13
    Changes: Data collection, Database references, Other, Refinement description