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Atomistry » Manganese » PDB 117e-1cev » 1ar4 » |
Manganese in PDB 1ar4: X-Ray Structure Analysis of the Cambialistic Superoxide Dismutase From Propionibacterium Shermanii Active with Fe or MnEnzymatic activity of X-Ray Structure Analysis of the Cambialistic Superoxide Dismutase From Propionibacterium Shermanii Active with Fe or Mn
All present enzymatic activity of X-Ray Structure Analysis of the Cambialistic Superoxide Dismutase From Propionibacterium Shermanii Active with Fe or Mn:
1.15.1.1; Protein crystallography data
The structure of X-Ray Structure Analysis of the Cambialistic Superoxide Dismutase From Propionibacterium Shermanii Active with Fe or Mn, PDB code: 1ar4
was solved by
M.Schmidt,
B.Meier,
F.Parak,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Manganese Binding Sites:
The binding sites of Manganese atom in the X-Ray Structure Analysis of the Cambialistic Superoxide Dismutase From Propionibacterium Shermanii Active with Fe or Mn
(pdb code 1ar4). This binding sites where shown within
5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the X-Ray Structure Analysis of the Cambialistic Superoxide Dismutase From Propionibacterium Shermanii Active with Fe or Mn, PDB code: 1ar4: Jump to Manganese binding site number: 1; 2; Manganese binding site 1 out of 2 in 1ar4Go back to Manganese Binding Sites List in 1ar4
Manganese binding site 1 out
of 2 in the X-Ray Structure Analysis of the Cambialistic Superoxide Dismutase From Propionibacterium Shermanii Active with Fe or Mn
Mono view Stereo pair view
Manganese binding site 2 out of 2 in 1ar4Go back to Manganese Binding Sites List in 1ar4
Manganese binding site 2 out
of 2 in the X-Ray Structure Analysis of the Cambialistic Superoxide Dismutase From Propionibacterium Shermanii Active with Fe or Mn
Mono view Stereo pair view
Reference:
M.Schmidt,
B.Meier,
F.Parak.
X-Ray Structure of the Cambialistic Superoxide Dismutase From Propionibacterium Shermanii Active with Fe or Mn J.Biol.Inorg.Chem. V. 1 532 1996.
Page generated: Tue Dec 15 03:46:11 2020
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