_EC 1.11.1.25 glutaredoxin-dependent peroxiredoxin. 3 PDB entries  
EC 1.-.-.- Oxidoreductases. [21,484 PDB entries]
EC 1.11.-.- Acting on a peroxide as acceptor. [1,313 PDB entries]
EC 1.11.1.- Peroxidases. [1,209 PDB entries]
EC 1.11.1.25 glutaredoxin-dependent peroxiredoxin. [3 PDB entries]
1tp9

Reaction: [glutaredoxin]-dithiol + a hydroperoxide = [glutaredoxin]-disulfide + an alcohol + H2O.
 

[glutaredoxin]-dithiol
 +
hydroperoxide
 = [glutaredoxin]-disulfide
 +
alcohol
 + H2O
Molecule diagrams generated from .mol files obtained from the KEGG ftp site.

Comments: Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant proteins. They can be divided into three classes: typical 2-Cys, atypical 2-Cys and 1-Cys peroxiredoxins . The peroxidase reaction comprises two steps centered around a redox- active cysteine called the peroxidatic cysteine. All three peroxiredoxin classes have the first step in common, in which the peroxidatic cysteine attacks the peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic acid). The second step of the peroxidase reaction, the regeneration of
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There are 3 PDB entries in enzyme class E.C.1.11.1.25

  PDB code Protein
1tp9
Prx d (type ii) from populus tremula
Source: Populus trichocarpa. Organism_taxid: 3694. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.
Chains: A, B, C, D (162 residues) CATH domain: 3.40.30.10
2pwj
Structure of a mitochondrial type ii peroxiredoxin from pisum sativum
Source: Pisum sativum. Garden pea. Gene: prx. Expressed in: escherichia coli.
Chains: A, B, C, D, E, F (162 residues) CATH domain: 3.40.30.10
5ykj
Structural basis of the thiol resolving mechanism in yeast mitochondrial 1-cys peroxiredoxin via glutathione/thioredoxin systems
Source: Saccharomyces cerevisiae (strain atcc 204508 / s288c). Baker's yeast. Organism_taxid: 559292. Strain: atcc 204508 / s288c. Gene: prx1, ybl064c, ybl0503, ybl0524. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chain: A (213 residues)