Atomistry » Iron » PDB 1c6o-1ch2 » 1ccb
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 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: 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:

Resolution Low / High (Å) N/A / 2.10
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 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 1ccb

Go back to Iron Binding Sites List in 1ccb
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:16.9
occ:1.00
 FE A:HEM295 0.0 16.9 1.0
NE2 A:HIS175 2.0 17.1 1.0
NA A:HEM295 2.0 15.7 1.0
NC A:HEM295 2.1 19.7 1.0
NB A:HEM295 2.1 18.9 1.0
ND A:HEM295 2.1 20.7 1.0
O A:HOH313 2.3 21.2 1.0
CE1 A:HIS175 2.7 18.6 1.0
C1A A:HEM295 3.0 20.2 1.0
C4B A:HEM295 3.0 16.8 1.0
C1C A:HEM295 3.0 19.6 1.0
C4D A:HEM295 3.0 16.4 1.0
C4A A:HEM295 3.1 19.0 1.0
C4C A:HEM295 3.1 24.4 1.0
C1B A:HEM295 3.1 19.9 1.0
C1D A:HEM295 3.1 17.2 1.0
CD2 A:HIS175 3.1 17.5 1.0
CHC A:HEM295 3.3 14.3 1.0
CHA A:HEM295 3.3 16.7 1.0
CHB A:HEM295 3.4 18.2 1.0
HE1 A:TRP51 3.4 0.0 1.0
CHD A:HEM295 3.4 19.4 1.0
ND1 A:HIS175 3.9 17.1 1.0
CG A:HIS175 4.2 16.1 1.0
C2A A:HEM295 4.2 18.8 1.0
C3B A:HEM295 4.2 20.5 1.0
NE1 A:TRP51 4.2 30.9 1.0
C3A A:HEM295 4.2 17.0 1.0
C3D A:HEM295 4.2 17.7 1.0
C3C A:HEM295 4.2 20.2 1.0
C2C A:HEM295 4.3 19.8 1.0
C2D A:HEM295 4.3 16.4 1.0
C2B A:HEM295 4.3 21.1 1.0
HE2 A:HIS52 4.5 0.0 1.0
O A:HOH300 4.5 41.7 1.0
CD1 A:TRP51 4.7 25.0 1.0
HD1 A:HIS175 4.7 0.0 1.0
HE A:ARG48 4.8 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: Sat Aug 3 03:14:03 2024

Last articles

Ca in 5J1Z
Ca in 5J03
Ca in 5IX0
Ca in 5IU9
Ca in 5IYZ
Ca in 5IWU
Ca in 5IRB
Ca in 5IWK
Ca in 5IWG
Ca in 5IV3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy