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PDBsum entry 4d73

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protein Protein-protein interface(s) links
Oxidoreductase PDB id
4d73

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
172 a.a.
170 a.a.
Waters ×234
PDB id:
4d73
Name: Oxidoreductase
Title: X-ray structure of a peroxiredoxin
Structure: 1-cys peroxiredoxin. Chain: a. Engineered: yes. Mutation: yes. 1-cys peroxiredoxin. Chain: b. Engineered: yes. Mutation: yes
Source: Plasmodium falciparum. Malaria parasite p. Falciparum. Organism_taxid: 5833. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.80Å     R-factor:   0.154     R-free:   0.195
Authors: V.Staudacher,C.F.Djuika,J.Koduka,S.Schlossarek,J.Kopp,M.Buechler, M.Lanzer,M.Deponte
Key ref: V.Staudacher et al. (2015). Plasmodium falciparum antioxidant protein reveals a novel mechanism for balancing turnover and inactivation of peroxiredoxins. Free Radic Biol Med, 85, 228-236. PubMed id: 25952724 DOI: 10.1016/j.freeradbiomed.2015.04.030
Date:
19-Nov-14     Release date:   13-May-15    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q5MYR6  (Q5MYR6_PLAF7) -  1-cys peroxiredoxin from Plasmodium falciparum (isolate 3D7)
Seq:
Struc:
240 a.a.
172 a.a.*
Protein chain
Pfam   ArchSchema ?
Q5MYR6  (Q5MYR6_PLAF7) -  1-cys peroxiredoxin from Plasmodium falciparum (isolate 3D7)
Seq:
Struc:
240 a.a.
170 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 5 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: Chains A, B: E.C.1.11.1.15  - Transferred entry: 1.11.1.24, 1.11.1.25, 1.11.1.26, 1.11.1.27, 1.11.1.28
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
Peroxiredoxin
      Reaction: 2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH
2 × R'-SH
+ ROOH
= R'-S-S-R'
+ H(2)O
+ ROH
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
DOI no: 10.1016/j.freeradbiomed.2015.04.030 Free Radic Biol Med 85:228-236 (2015)
PubMed id: 25952724  
 
 
Plasmodium falciparum antioxidant protein reveals a novel mechanism for balancing turnover and inactivation of peroxiredoxins.
V.Staudacher, C.F.Djuika, J.Koduka, S.Schlossarek, J.Kopp, M.Büchler, M.Lanzer, M.Deponte.
 
  ABSTRACT  
 
No abstract given.

 

 

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