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PDBsum entry 1sod

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Oxidoreductase (superoxide acceptor) PDB id
1sod
Jmol
Contents
Protein chain
151 a.a.*
Metals
_ZN
_CU
* C-alpha coords only
Superseded by: 2sod 2sod
PDB id:
1sod
Name: Oxidoreductase (superoxide acceptor)
Structure: Cu,zn superoxide dismutase
Source: Cow (bos taurus)
Authors: J.S.Richardson,K.A.Thomas,D.C.Richardson
Key ref: J.S.Richardson et al. (1975). Alpha-carbon coordinates for bovine Cu,Zn superoxide dismutase. Biochem Biophys Res Commun, 63, 986-992. PubMed id: 1169067
Date:
01-Aug-75    
 Headers
 References

Protein chain
No UniProt id for this chain
Struc: 151 a.a.
Key:    Secondary structure

 

 
    Key reference    
 
 
Biochem Biophys Res Commun 63:986-992 (1975)
PubMed id: 1169067  
 
 
Alpha-carbon coordinates for bovine Cu,Zn superoxide dismutase.
J.S.Richardson, K.A.Thomas, D.C.Richardson.
 
  ABSTRACT  
 

 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21127923 J.M.Ouyang, X.Q.Yao, J.Tan, and F.X.Wang (2011).
Renal epithelial cell injury and its promoting role in formation of calcium oxalate monohydrate.
  J Biol Inorg Chem, 16, 405-416.  
7703375 H.Zaima, N.Ueyama, H.Adachi, and A.Nakamura (1995).
1H-, 13C-, and 113Cd-NMR study of the Cd(II) complex of a blocked peptide, Z-Cys-Ala-Pro-His-OMe, in organic solvents.
  Biopolymers, 35, 319-329.  
2594778 X.W.Wu, C.C.Lee, D.M.Muzny, and C.T.Caskey (1989).
Urate oxidase: primary structure and evolutionary implications.
  Proc Natl Acad Sci U S A, 86, 9412-9416.  
6378653 J.L.Dreyer (1984).
Electron transfer in biological systems: an overview.
  Experientia, 40, 653-675.  
6328509 S.Kubota, and J.T.Yang (1984).
Bis[cyclo(histidylhistidine)]copper(II) complex that mimicks the active center of superoxide dismutase has its catalytic activity.
  Proc Natl Acad Sci U S A, 81, 3283-3286.  
7374781 A.D.McLachlan (1980).
Repeated folding pattern in copper-zinc superoxide dismutase.
  Nature, 285, 267-268.  
41239 J.S.Valentine, M.W.Pantoliano, P.J.McDonnell, A.R.Burger, and S.J.Lippard (1979).
pH-dependent migration of copper(II) to the vacant zinc-binding site of zinc-free bovine erythrocyte superoxide dismutase.
  Proc Natl Acad Sci U S A, 76, 4245-4249.  
270659 C.Chothia, M.Levitt, and D.Richardson (1977).
Structure of proteins: packing of alpha-helices and pleated sheets.
  Proc Natl Acad Sci U S A, 74, 4130-4134.  
949976 S.Marklund, G.Beckman, and T.Stigbrand (1976).
A comparison between the common type and a rare genetic variant of human cupro-zinc superoxide dismutase.
  Eur J Biochem, 65, 415-422.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.