PDBsum entry 1dt0

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Oxidoreductase PDB id
Protein chains
197 a.a. *
_FE ×3
Waters ×566
* Residue conservation analysis
PDB id:
Name: Oxidoreductase
Title: Cloning, sequence, and crystallographic structure of recombinant iron superoxide dismutase from pseudomonas ovalis
Structure: Superoxide dismutase. Chain: a, b, c. Engineered: yes
Source: Pseudomonas putida. Organism_taxid: 303. Expressed in: escherichia coli. Expression_system_taxid: 562. Plasmid library
Biol. unit: Dimer (from PDB file)
2.10Å     R-factor:   0.220     R-free:   0.290
Authors: C.J.Bond,J.Huang,R.Hajduk,K.Flick,P.Heath,B.L.Stoddard
Key ref:
C.J.Bond et al. (2000). Cloning, sequence and crystallographic structure of recombinant iron superoxide dismutase from Pseudomonas ovalis. Acta Crystallogr D Biol Crystallogr, 56, 1359-1366. PubMed id: 11053832 DOI: 10.1107/S0907444900009537
10-Jan-00     Release date:   20-Dec-00    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
P09223  (SODF_PSEPU) -  Superoxide dismutase [Fe]
198 a.a.
197 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 4 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.  - Superoxide dismutase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: 2 superoxide + 2 H+ = O2 + H2O2
2 × superoxide
+ 2 × H(+)
= O(2)
+ H(2)O(2)
      Cofactor: Fe cation or Mn(2+) or (Zn(2+) and Cu cation)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     oxidation-reduction process   3 terms 
  Biochemical function     oxidoreductase activity     3 terms  


    Added reference    
DOI no: 10.1107/S0907444900009537 Acta Crystallogr D Biol Crystallogr 56:1359-1366 (2000)
PubMed id: 11053832  
Cloning, sequence and crystallographic structure of recombinant iron superoxide dismutase from Pseudomonas ovalis.
C.J.Bond, J.Huang, R.Hajduk, K.E.Flick, P.J.Heath, B.L.Stoddard.
The gene encoding the iron-dependent superoxide dismutase from Pseudomonas ovalis was cloned from a genomic library and sequenced. The ORF differs from the previously published protein sequence, which was used for the original structure determination, at 16 positions. The differences include three additional inserted residues, one deleted residue and 12 point substitutions. The gene was subcloned and the recombinant protein overexpressed, purified and crystallized in a trigonal space group. The structure was determined by molecular replacement and was refined to 2.1 A resolution.
  Selected figure(s)  
Figure 2.
Figure 2 Structure of an SOD monomer. Side chains are shown where the sequence of the protein deviates from the original model. The N-terminal Met is not observed in the electron-density maps.
  The above figure is reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2000, 56, 1359-1366) copyright 2000.  
  Figure was selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
12392545 T.Hunter, J.V.Bannister, and G.J.Hunter (2002).
Thermostability of manganese- and iron-superoxide dismutases from Escherichia coli is determined by the characteristic position of a glutamine residue.
  Eur J Biochem, 269, 5137-5148.  
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