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Iron in PDB 3exb: Crystal Structure of Cytochrome C Peroxidase with A Proposed Electron Pathway Excised in A Complex with A Peptide Wire

Enzymatic activity of Crystal Structure of Cytochrome C Peroxidase with A Proposed Electron Pathway Excised in A Complex with A Peptide Wire

All present enzymatic activity of Crystal Structure of Cytochrome C Peroxidase with A Proposed Electron Pathway Excised in A Complex with A Peptide Wire:
1.11.1.5;

Protein crystallography data

The structure of Crystal Structure of Cytochrome C Peroxidase with A Proposed Electron Pathway Excised in A Complex with A Peptide Wire, PDB code: 3exb was solved by A.-M.A.Putnam, Y.-T.Lee, D.B.Goodin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.60
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 107.029, 75.070, 50.790, 90.00, 90.00, 90.00
R / Rfree (%) 16.8 / 19

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Cytochrome C Peroxidase with A Proposed Electron Pathway Excised in A Complex with A Peptide Wire (pdb code 3exb). 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 Crystal Structure of Cytochrome C Peroxidase with A Proposed Electron Pathway Excised in A Complex with A Peptide Wire, PDB code: 3exb:

Iron binding site 1 out of 1 in 3exb

Go back to Iron Binding Sites List in 3exb
Iron binding site 1 out of 1 in the Crystal Structure of Cytochrome C Peroxidase with A Proposed Electron Pathway Excised in A Complex with A Peptide Wire


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of Cytochrome C Peroxidase with A Proposed Electron Pathway Excised in A Complex with A Peptide Wire within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe300

b:6.4
occ:1.00
 FE A:HEM300 0.0 6.4 1.0
NB A:HEM300 2.0 5.6 1.0
NA A:HEM300 2.0 5.3 1.0
O A:HOH860 2.0 21.1 1.0
NC A:HEM300 2.1 5.3 1.0
ND A:HEM300 2.1 5.0 1.0
NE2 A:HIS175 2.1 14.2 1.0
C4B A:HEM300 3.0 3.9 1.0
C1D A:HEM300 3.1 5.6 1.0
C1A A:HEM300 3.1 5.2 1.0
C4D A:HEM300 3.1 3.9 1.0
C4A A:HEM300 3.1 4.9 1.0
CE1 A:HIS175 3.1 13.6 1.0
C1C A:HEM300 3.1 2.8 1.0
C1B A:HEM300 3.1 6.2 1.0
C4C A:HEM300 3.1 5.9 1.0
CD2 A:HIS175 3.1 13.3 1.0
CHC A:HEM300 3.4 4.3 1.0
CHA A:HEM300 3.4 4.1 1.0
CHD A:HEM300 3.5 4.8 1.0
CHB A:HEM300 3.5 4.4 1.0
NE1 A:TRP51 4.0 15.1 1.0
ND1 A:HIS175 4.2 12.8 1.0
NE A:ARG48 4.2 19.3 0.5
O A:HOH586 4.2 12.2 1.0
C3B A:HEM300 4.3 5.2 1.0
C2D A:HEM300 4.3 6.2 1.0
C3A A:HEM300 4.3 5.0 1.0
CG A:HIS175 4.3 12.1 1.0
C2B A:HEM300 4.3 5.6 1.0
C2A A:HEM300 4.3 4.5 1.0
C3D A:HEM300 4.3 5.1 1.0
C2C A:HEM300 4.3 4.1 1.0
C3C A:HEM300 4.3 5.8 1.0
CD1 A:TRP51 4.4 13.1 1.0
NH1 A:ARG48 4.6 12.2 0.5
C4 B:EXB293 4.8 7.8 1.0
CZ A:ARG48 4.9 18.6 0.5
C5 B:EXB293 5.0 9.3 1.0

Reference:

A.M.Hays Putnam, Y.T.Lee, D.B.Goodin. Replacement of An Electron Transfer Pathway in Cytochrome C Peroxidase with A Surrogate Peptide Biochemistry V. 48 1 2009.
ISSN: ISSN 0006-2960
PubMed: 19072042
DOI: 10.1021/BI8020263
Page generated: Tue Aug 5 01:06:52 2025

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