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Atomistry » Iron » PDB 1c6o-1ch2 » 1ccb » |
Iron in PDB 1ccb: The Asp-His-Fe Triad of Cytochrome C Peroxidase Controls the Reduction Potential, Electronic Structure, and Coupling of the Tryptophan Free- Radical to the HemeEnzymatic activity of The Asp-His-Fe Triad of Cytochrome C Peroxidase Controls the Reduction Potential, Electronic Structure, and Coupling of the Tryptophan Free- Radical to the Heme
All present enzymatic activity of The Asp-His-Fe Triad of Cytochrome C Peroxidase Controls the Reduction Potential, Electronic Structure, and Coupling of the Tryptophan Free- Radical to the Heme:
1.11.1.5; Protein crystallography data
The structure of The Asp-His-Fe Triad of Cytochrome C Peroxidase Controls the Reduction Potential, Electronic Structure, and Coupling of the Tryptophan Free- Radical to the Heme, PDB code: 1ccb
was solved by
D.B.Goodin,
D.E.Mcree,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Iron Binding Sites:
The binding sites of Iron atom in the The Asp-His-Fe Triad of Cytochrome C Peroxidase Controls the Reduction Potential, Electronic Structure, and Coupling of the Tryptophan Free- Radical to the Heme
(pdb code 1ccb). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the The Asp-His-Fe Triad of Cytochrome C Peroxidase Controls the Reduction Potential, Electronic Structure, and Coupling of the Tryptophan Free- Radical to the Heme, PDB code: 1ccb: Iron binding site 1 out of 1 in 1ccbGo back to![]() ![]()
Iron binding site 1 out
of 1 in the The Asp-His-Fe Triad of Cytochrome C Peroxidase Controls the Reduction Potential, Electronic Structure, and Coupling of the Tryptophan Free- Radical to the Heme
![]() Mono view ![]() Stereo pair view
Reference:
D.B.Goodin,
D.E.Mcree.
The Asp-His-Fe Triad of Cytochrome C Peroxidase Controls the Reduction Potential, Electronic Structure, and Coupling of the Tryptophan Free Radical to the Heme. Biochemistry V. 32 3313 1993.
Page generated: Sat Aug 3 03:14:03 2024
ISSN: ISSN 0006-2960 PubMed: 8384877 DOI: 10.1021/BI00064A014 |
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