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Iron in PDB 1h5m: X-Ray Induced Reduction of Horseradish Peroxidase C1A Compound III (0-100% Dose)

Enzymatic activity of X-Ray Induced Reduction of Horseradish Peroxidase C1A Compound III (0-100% Dose)

All present enzymatic activity of X-Ray Induced Reduction of Horseradish Peroxidase C1A Compound III (0-100% Dose):
1.11.1.7;

Protein crystallography data

The structure of X-Ray Induced Reduction of Horseradish Peroxidase C1A Compound III (0-100% Dose), PDB code: 1h5m 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) 38.16 / 1.57
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 40.352, 67.513, 117.304, 90.00, 90.00, 90.00
R / Rfree (%) 17.7 / 19.8

Other elements in 1h5m:

The structure of X-Ray Induced Reduction of Horseradish Peroxidase C1A Compound III (0-100% Dose) also contains other interesting chemical elements:

Calcium (Ca) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the X-Ray Induced Reduction of Horseradish Peroxidase C1A Compound III (0-100% Dose) (pdb code 1h5m). 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 X-Ray Induced Reduction of Horseradish Peroxidase C1A Compound III (0-100% Dose), PDB code: 1h5m:

Iron binding site 1 out of 1 in 1h5m

Go back to Iron Binding Sites List in 1h5m
Iron binding site 1 out of 1 in the X-Ray Induced Reduction of Horseradish Peroxidase C1A Compound III (0-100% Dose)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of X-Ray Induced Reduction of Horseradish Peroxidase C1A Compound III (0-100% Dose) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe350

b:7.0
occ:1.00
 FE A:HEM350 0.0 7.0 1.0
ND A:HEM350 2.0 7.5 1.0
NA A:HEM350 2.0 6.9 1.0
NB A:HEM350 2.0 5.1 1.0
NC A:HEM350 2.0 5.7 1.0
NE2 A:HIS170 2.1 6.0 1.0
C1D A:HEM350 3.0 7.7 1.0
C1B A:HEM350 3.0 7.0 1.0
C4A A:HEM350 3.0 8.5 1.0
CE1 A:HIS170 3.1 6.3 1.0
C4B A:HEM350 3.1 6.2 1.0
C4C A:HEM350 3.1 6.5 1.0
C1C A:HEM350 3.1 5.5 1.0
C4D A:HEM350 3.1 8.5 1.0
C1A A:HEM350 3.1 8.9 1.0
CD2 A:HIS170 3.1 6.7 1.0
CHD A:HEM350 3.4 7.2 1.0
CHC A:HEM350 3.4 6.7 1.0
CHB A:HEM350 3.4 7.6 1.0
CHA A:HEM350 3.4 7.5 1.0
ND1 A:HIS170 4.2 5.8 1.0
CG A:HIS170 4.2 7.5 1.0
C2D A:HEM350 4.3 8.3 1.0
C2B A:HEM350 4.3 6.6 1.0
C3A A:HEM350 4.3 8.3 1.0
C3D A:HEM350 4.3 8.6 1.0
C3B A:HEM350 4.3 6.8 1.0
C2A A:HEM350 4.3 8.7 1.0
C2C A:HEM350 4.3 6.0 1.0
C3C A:HEM350 4.3 5.9 1.0
NE A:ARG38 4.3 9.8 1.0
CE2 A:PHE41 4.5 8.8 1.0
CG A:ARG38 4.8 10.1 1.0
CD2 A:PHE41 4.8 8.0 1.0
CD A:ARG38 4.8 8.2 1.0
CZ A:PHE221 4.9 8.6 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: Sat Aug 3 07:16:57 2024

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