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Iron in PDB 1cpe: A Cation Binding Motif Stabilizes the Compound I Radical of Cytochrome C Peroxidase

Enzymatic activity of A Cation Binding Motif Stabilizes the Compound I Radical of Cytochrome C Peroxidase

All present enzymatic activity of A Cation Binding Motif Stabilizes the Compound I Radical of Cytochrome C Peroxidase:
1.11.1.5;

Protein crystallography data

The structure of A Cation Binding Motif Stabilizes the Compound I Radical of Cytochrome C Peroxidase, PDB code: 1cpe was solved by M.A.Miller, G.W.Han, J.Kraut, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.20
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 105.020, 74.250, 45.140, 90.00, 90.00, 90.00
R / Rfree (%) n/a / n/a

Other elements in 1cpe:

The structure of A Cation Binding Motif Stabilizes the Compound I Radical of Cytochrome C Peroxidase also contains other interesting chemical elements:

Potassium (K) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the A Cation Binding Motif Stabilizes the Compound I Radical of Cytochrome C Peroxidase (pdb code 1cpe). 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 A Cation Binding Motif Stabilizes the Compound I Radical of Cytochrome C Peroxidase, PDB code: 1cpe:

Iron binding site 1 out of 1 in 1cpe

Go back to Iron Binding Sites List in 1cpe
Iron binding site 1 out of 1 in the A Cation Binding Motif Stabilizes the Compound I Radical of Cytochrome C Peroxidase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of A Cation Binding Motif Stabilizes the Compound I Radical of Cytochrome C Peroxidase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe296

b:20.8
occ:1.00
 FE A:HEM296 0.0 20.8 1.0
O A:HOH595 1.9 12.0 1.0
NC A:HEM296 1.9 18.7 1.0
NA A:HEM296 1.9 12.7 1.0
NB A:HEM296 2.0 15.9 1.0
ND A:HEM296 2.0 20.5 1.0
NE2 A:HIS175 2.0 21.3 1.0
C1D A:HEM296 2.9 18.8 1.0
C4C A:HEM296 2.9 19.1 1.0
C1A A:HEM296 2.9 15.9 1.0
CE1 A:HIS175 3.0 19.5 1.0
C4B A:HEM296 3.0 14.2 1.0
C4A A:HEM296 3.0 13.8 1.0
C1C A:HEM296 3.0 20.4 1.0
C4D A:HEM296 3.0 13.6 1.0
C1B A:HEM296 3.1 14.6 1.0
CD2 A:HIS175 3.1 22.4 1.0
CHD A:HEM296 3.2 15.8 1.0
CHC A:HEM296 3.4 16.8 1.0
CHA A:HEM296 3.5 11.8 1.0
CHB A:HEM296 3.6 11.8 1.0
NE1 A:TRP51 4.0 26.3 1.0
C3C A:HEM296 4.1 21.4 1.0
ND1 A:HIS175 4.1 16.6 1.0
O A:HOH445 4.1 54.7 1.0
C2D A:HEM296 4.2 18.7 1.0
C2A A:HEM296 4.2 20.5 1.0
CG A:HIS175 4.2 22.3 1.0
C3A A:HEM296 4.2 16.5 1.0
C2C A:HEM296 4.2 19.8 1.0
C3B A:HEM296 4.2 16.3 1.0
C3D A:HEM296 4.2 19.7 1.0
C2B A:HEM296 4.3 16.0 1.0
O A:HOH596 4.3 54.9 1.0
NE A:ARG48 4.3 36.2 1.0
CD1 A:TRP51 4.6 27.2 1.0
O A:HOH979 4.7 23.8 1.0
CG A:ARG48 4.9 27.2 1.0
NH2 A:ARG48 5.0 30.5 1.0
CE2 A:TRP51 5.0 26.6 1.0

Reference:

M.A.Miller, G.W.Han, J.Kraut. A Cation Binding Motif Stabilizes the Compound I Radical of Cytochrome C Peroxidase. Proc.Natl.Acad.Sci.Usa V. 91 11118 1994.
ISSN: ISSN 0027-8424
PubMed: 7972020
DOI: 10.1073/PNAS.91.23.11118
Page generated: Wed Jul 16 13:04:23 2025

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