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Iron in PDB 1h5a: Structure of Ferric Horseradish Peroxidase C1A in Complex with Acetate

Enzymatic activity of Structure of Ferric Horseradish Peroxidase C1A in Complex with Acetate

All present enzymatic activity of Structure of Ferric Horseradish Peroxidase C1A in Complex with Acetate:
1.11.1.7;

Protein crystallography data

The structure of Structure of Ferric Horseradish Peroxidase C1A in Complex with Acetate, PDB code: 1h5a was solved by G.I.Berglund, G.H.Carlsson, J.Hajdu, A.T.Smith, H.Szoke, A.Henriksen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.71 / 1.6
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 40.347, 67.774, 117.265, 90.00, 90.00, 90.00
R / Rfree (%) 17.8 / 20.2

Other elements in 1h5a:

The structure of Structure of Ferric Horseradish Peroxidase C1A in Complex with Acetate also contains other interesting chemical elements:

Calcium (Ca) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Structure of Ferric Horseradish Peroxidase C1A in Complex with Acetate (pdb code 1h5a). 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 Structure of Ferric Horseradish Peroxidase C1A in Complex with Acetate, PDB code: 1h5a:

Iron binding site 1 out of 1 in 1h5a

Go back to Iron Binding Sites List in 1h5a
Iron binding site 1 out of 1 in the Structure of Ferric Horseradish Peroxidase C1A in Complex with Acetate


Mono view


Stereo pair view

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

b:9.3
occ:1.00
 FE A:HEM350 0.0 9.3 1.0
ND A:HEM350 2.0 9.5 1.0
NA A:HEM350 2.0 9.4 1.0
NB A:HEM350 2.0 6.4 1.0
NC A:HEM350 2.0 8.5 1.0
NE2 A:HIS170 2.1 8.8 1.0
C1D A:HEM350 3.0 11.0 1.0
C4A A:HEM350 3.1 9.1 1.0
CE1 A:HIS170 3.1 8.9 1.0
C1B A:HEM350 3.1 7.8 1.0
C4D A:HEM350 3.1 11.7 1.0
C4B A:HEM350 3.1 8.2 1.0
C4C A:HEM350 3.1 9.9 1.0
C1C A:HEM350 3.1 8.4 1.0
C1A A:HEM350 3.1 10.5 1.0
CD2 A:HIS170 3.1 10.8 1.0
CHD A:HEM350 3.4 10.1 1.0
CHC A:HEM350 3.4 9.1 1.0
CHB A:HEM350 3.4 7.6 1.0
CHA A:HEM350 3.4 10.6 1.0
O A:ACT501 3.6 19.1 1.0
ND1 A:HIS170 4.2 9.1 1.0
C2D A:HEM350 4.3 10.5 1.0
CG A:HIS170 4.3 9.7 1.0
C3D A:HEM350 4.3 10.5 1.0
C2B A:HEM350 4.3 7.9 1.0
C3A A:HEM350 4.3 8.1 1.0
C3B A:HEM350 4.3 8.5 1.0
C2A A:HEM350 4.3 9.9 1.0
C2C A:HEM350 4.3 9.7 1.0
C3C A:HEM350 4.3 9.3 1.0
C A:ACT501 4.4 17.0 1.0
CE2 A:PHE41 4.5 10.4 1.0
NE A:ARG38 4.6 10.6 1.0
CZ A:PHE221 4.8 10.8 1.0
CD2 A:PHE41 4.9 10.3 1.0
CG A:ARG38 5.0 13.2 1.0
CD A:ARG38 5.0 10.9 1.0

Reference:

G.I.Berglund, G.H.Carlsson, A.T.Smith, H.Szoke, A.Henriksen, J.Hajdu. The Catalytic Pathway of Horseradish Peroxidase at High Resolution Nature V. 417 463 2002.
ISSN: ISSN 0028-0836
PubMed: 12024218
DOI: 10.1038/417463A
Page generated: Sun Dec 13 14:16:50 2020

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