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Iron in PDB 1ccc: 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

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

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: 1ccc was solved by D.B.Goodin, D.E.Mcree, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 105.200, 74.300, 45.400, 90.00, 90.00, 90.00
R / Rfree (%) 19 / n/a

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 1ccc). 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: 1ccc:

Iron binding site 1 out of 1 in 1ccc

Go back to Iron Binding Sites List in 1ccc
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

A full contact list of Iron with other atoms in the Fe binding site number 1 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 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe295

b:14.2
occ:1.00
 FE A:HEM295 0.0 14.2 1.0
O A:HOH313 1.9 11.7 1.0
NE2 A:HIS175 2.0 20.3 1.0
NC A:HEM295 2.0 13.0 1.0
NA A:HEM295 2.1 12.9 1.0
NB A:HEM295 2.1 13.5 1.0
ND A:HEM295 2.1 16.8 1.0
CE1 A:HIS175 2.9 20.2 1.0
C4B A:HEM295 3.0 12.4 1.0
C1C A:HEM295 3.0 15.2 1.0
C1A A:HEM295 3.0 16.6 1.0
C4D A:HEM295 3.0 16.1 1.0
CD2 A:HIS175 3.0 20.4 1.0
C4C A:HEM295 3.1 13.6 1.0
C1D A:HEM295 3.1 16.1 1.0
C4A A:HEM295 3.1 13.6 1.0
C1B A:HEM295 3.1 13.4 1.0
CHC A:HEM295 3.3 8.8 1.0
CHA A:HEM295 3.4 14.7 1.0
CHD A:HEM295 3.4 13.4 1.0
CHB A:HEM295 3.4 12.5 1.0
HE1 A:TRP51 3.6 0.0 1.0
ND1 A:HIS175 4.0 21.0 1.0
CG A:HIS175 4.2 19.1 1.0
O A:HOH300 4.2 38.7 1.0
NE1 A:TRP51 4.2 20.0 1.0
C2A A:HEM295 4.2 14.6 1.0
C3C A:HEM295 4.2 14.2 1.0
C3D A:HEM295 4.2 19.5 1.0
C3B A:HEM295 4.2 15.4 1.0
C3A A:HEM295 4.2 10.9 1.0
C2C A:HEM295 4.2 13.6 1.0
C2D A:HEM295 4.3 17.1 1.0
C2B A:HEM295 4.3 16.4 1.0
CD1 A:TRP51 4.6 18.6 1.0
O A:HOH344 4.6 37.1 1.0
HD1 A:HIS175 4.9 0.0 1.0
HE A:ARG48 4.9 0.0 1.0

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.
ISSN: ISSN 0006-2960
PubMed: 8384877
DOI: 10.1021/BI00064A014
Page generated: Wed Jul 16 12:54:18 2025

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