PDBsum entry 3hw7

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protein metals Protein-protein interface(s) links
Oxidoreductase, metal binding protein PDB id
Protein chains
151 a.a. *
_ZN ×2
CU1 ×2
Waters ×206
* Residue conservation analysis
PDB id:
Name: Oxidoreductase, metal binding protein
Title: High pressure (0.57 gpa) crystal structure of bovine copper, superoxide dismutase at 2.0 angstroms
Structure: Superoxide dismutase [cu-zn]. Chain: a, b. Ec:
Source: Bos taurus. Bovine. Organism_taxid: 9913. Cell: erythrocytes
2.00Å     R-factor:   0.174     R-free:   0.218
Authors: I.Ascone,C.Savino
Key ref: I.Ascone et al. (2010). Flexibility of the Cu,Zn superoxide dismutase structure investigated at 0.57 GPa. Acta Crystallogr D Biol Crystallogr, 66, 654-663. PubMed id: 20516618
17-Jun-09     Release date:   23-Jun-10    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
P00442  (SODC_BOVIN) -  Superoxide dismutase [Cu-Zn]
152 a.a.
151 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 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: Iron or manganese or (zinc and copper)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     protein complex   11 terms 
  Biological process     reactive oxygen species metabolic process   45 terms 
  Biochemical function     antioxidant activity     10 terms  


    Added reference    
Acta Crystallogr D Biol Crystallogr 66:654-663 (2010)
PubMed id: 20516618  
Flexibility of the Cu,Zn superoxide dismutase structure investigated at 0.57 GPa.
I.Ascone, C.Savino, R.Kahn, R.Fourme.
The 2 A resolution crystal structure of bovine erythrocyte Cu,Zn superoxide dismutase (CuZnSOD) has been determined by X-ray diffraction at high pressure (0.57 GPa) and room temperature. At 0.57 GPa the secondary, tertiary and quaternary structures are similar to other previously determined bovine erythrocyte CuZnSOD structures. Nevertheless, pressure has a localized impact on the atomic coordinates of C(alpha) atoms and on side chains. The compression of the crystal and of the protein backbone is anisotropic. This anisotropy is discussed, taking into account intermolecular contacts and protein conformation. Pressure perturbation highlights the more flexible zones in the protein such as the electrostatic loop. At 0.57 GPa, a global shift of the dimetallic sites in both subunits and changes in the oxidation state of Cu were observed. The flexibility of the electrostatic loop may be useful for the interaction of different metal carriers in the copper-uptake process, whereas the flexibility of the metal sites involved in the activity of the protein could contribute to explaining the ubiquitous character of CuZnSODs, which are found in organisms living in very different conditions, including the deep-sea environment. This work illustrates the potential of combining X-ray crystallography with high pressure to promote and stabilize higher energy conformational substates.