Brand  (β version)

PDB ID: 1H4O

Hetero Atom Contents

  The number of atoms exceeds 100,000.
  So, it can not be displayed here.

Select unit:

Select hetatm:   

close
information
centroid:
interaction residue:

Select chain:   Sequence  

Data format:   

Color scheme of protein:

Ligands
Code Name Style Show Link
BEZ Benzoic acid PoSSuM
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show

Structure summary

Code : 1H4O   PDBj   RCSB PDB   PDBe
Header : OXIDOREDUCTASE
Title : Monoclinic form of human peroxiredoxin 5
Release Data : 2001-10-23
Compound :
mol_id molecule chains synonym
1 PEROXIREDOXIN 5 A,B,C,D,E,F,G,H PRDX5, PRXV, AOEB166, PMP20, ARC1
ec: 1.11.1.15
fragment: RESIDUES 54-214
Source :
mol_id organism_scientific organism_common expression_system
1 HOMO SAPIENS  (taxid:9606) HUMAN ESCHERICHIA COLI M15  (taxid:1007065)
organ: LUNG
expression_system_vector_type: PLASMID
expression_system_plasmid: PQE-30
Authors : Declercq, J.P., Evrard, C.
Keywords : ANTIOXIDANT ENZYME, THIOREDOXIN PEROTHIOREDOXIN, FOLDXIDASE, OXIDOREDUCTASE
Exp. method : X-RAY DIFFRACTION ( 1.95 Å )
Citation :

Crystal Structure of Human Peroxiredoxin 5, a Novel Type of Mammalian Peroxiredoxin at 1.5 A Resolution

Declercq, J.P.,Evrard, C.,Clippe, A.  et al.
(2001)  J.Mol.Biol.  311 : 751

PubMed: 11518528
DOI: 10.1006/JMBI.2001.4853

Cloning and Characterization of Aoeb166, a Novel Mammalian Antioxidant Enzyme of the Peroxiredoxin Family

Knoops, B.,Clippe, A.,Bogard, C.  et al.
(1999)  J.Biol.Chem.  274 : 30451

PubMed: 10521424
DOI: 10.1074/JBC.274.43.30451

Reaction

Chain : A, B, C, D, E, F, G, H
UniProt : P30044 (PRDX5_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]- disulfide + an alcohol + H2O 1.11.1.24 PubMed:10751410
-