Iron in PDB 7atj: Recombinant Horseradish Peroxidase C1A Complex with Cyanide and Ferulic Acid

Enzymatic activity of Recombinant Horseradish Peroxidase C1A Complex with Cyanide and Ferulic Acid

All present enzymatic activity of Recombinant Horseradish Peroxidase C1A Complex with Cyanide and Ferulic Acid:
1.11.1.7;

Protein crystallography data

The structure of Recombinant Horseradish Peroxidase C1A Complex with Cyanide and Ferulic Acid, PDB code: 7atj was solved by A.Henriksen, A.T.Smith, M.Gajhede, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 34.00 / 1.47
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 40.868, 66.930, 119.017, 90.00, 90.00, 90.00
R / Rfree (%) 16 / 20.3

Other elements in 7atj:

The structure of Recombinant Horseradish Peroxidase C1A Complex with Cyanide and Ferulic Acid also contains other interesting chemical elements:

Calcium (Ca) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Recombinant Horseradish Peroxidase C1A Complex with Cyanide and Ferulic Acid (pdb code 7atj). 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 Recombinant Horseradish Peroxidase C1A Complex with Cyanide and Ferulic Acid, PDB code: 7atj:

Iron binding site 1 out of 1 in 7atj

Go back to Iron Binding Sites List in 7atj
Iron binding site 1 out of 1 in the Recombinant Horseradish Peroxidase C1A Complex with Cyanide and Ferulic Acid


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Recombinant Horseradish Peroxidase C1A Complex with Cyanide and Ferulic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe350

b:6.8
occ:1.00
 FE A:HEM350 0.0 6.8 1.0
C A:CYN601 2.0 9.9 1.0
NB A:HEM350 2.0 6.6 1.0
NA A:HEM350 2.0 8.1 1.0
NC A:HEM350 2.0 7.8 1.0
ND A:HEM350 2.0 8.5 1.0
NE2 A:HIS170 2.1 8.1 1.0
CE1 A:HIS170 3.0 8.0 1.0
C1B A:HEM350 3.0 5.7 1.0
C1D A:HEM350 3.1 8.5 1.0
C4A A:HEM350 3.1 8.4 1.0
C4B A:HEM350 3.1 6.4 1.0
C4C A:HEM350 3.1 7.4 1.0
C1A A:HEM350 3.1 7.3 1.0
C1C A:HEM350 3.1 6.5 1.0
C4D A:HEM350 3.1 9.1 1.0
N A:CYN601 3.1 10.6 1.0
CD2 A:HIS170 3.2 7.4 1.0
CHA A:HEM350 3.4 8.0 1.0
CHC A:HEM350 3.4 7.6 1.0
CHB A:HEM350 3.5 5.7 1.0
CHD A:HEM350 3.5 5.8 1.0
ND1 A:HIS170 4.1 7.6 1.0
C2D A:HEM350 4.2 7.0 1.0
C2B A:HEM350 4.3 5.0 1.0
CG A:HIS170 4.3 8.6 1.0
C3B A:HEM350 4.3 5.9 1.0
C2A A:HEM350 4.3 6.8 1.0
C3A A:HEM350 4.3 8.2 1.0
C3D A:HEM350 4.3 7.7 1.0
C2C A:HEM350 4.3 7.3 1.0
C3C A:HEM350 4.4 5.8 1.0
CE2 A:PHE41 4.5 8.5 1.0
NE A:ARG38 4.6 8.3 1.0
CD A:ARG38 4.8 9.2 1.0
CD2 A:PHE41 4.8 6.9 1.0
CZ A:PHE221 4.9 9.7 1.0

Reference:

A.Henriksen, A.T.Smith, M.Gajhede. The Structures of the Horseradish Peroxidase C-Ferulic Acid Complex and the Ternary Complex with Cyanide Suggest How Peroxidases Oxidize Small Phenolic Substrates. J.Biol.Chem. V. 274 35005 1999.
ISSN: ISSN 0021-9258
PubMed: 10574977
DOI: 10.1074/JBC.274.49.35005
Page generated: Sun Dec 13 18:36:16 2020

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