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Iron in PDB 1kzm: Distal Heme Pocket Mutant (R38S/H42E) of Recombinant Horseradish Peroxidase C (Hrp C).

Enzymatic activity of Distal Heme Pocket Mutant (R38S/H42E) of Recombinant Horseradish Peroxidase C (Hrp C).

All present enzymatic activity of Distal Heme Pocket Mutant (R38S/H42E) of Recombinant Horseradish Peroxidase C (Hrp C).:
1.11.1.7;

Protein crystallography data

The structure of Distal Heme Pocket Mutant (R38S/H42E) of Recombinant Horseradish Peroxidase C (Hrp C)., PDB code: 1kzm was solved by K.Meno, 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) 20.00 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 40.400, 66.700, 117.100, 90.00, 90.00, 90.00
R / Rfree (%) 16.8 / 20.3

Other elements in 1kzm:

The structure of Distal Heme Pocket Mutant (R38S/H42E) of Recombinant Horseradish Peroxidase C (Hrp C). also contains other interesting chemical elements:

Arsenic (As) 1 atom
Calcium (Ca) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Distal Heme Pocket Mutant (R38S/H42E) of Recombinant Horseradish Peroxidase C (Hrp C). (pdb code 1kzm). 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 Distal Heme Pocket Mutant (R38S/H42E) of Recombinant Horseradish Peroxidase C (Hrp C)., PDB code: 1kzm:

Iron binding site 1 out of 1 in 1kzm

Go back to Iron Binding Sites List in 1kzm
Iron binding site 1 out of 1 in the Distal Heme Pocket Mutant (R38S/H42E) of Recombinant Horseradish Peroxidase C (Hrp C).


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Distal Heme Pocket Mutant (R38S/H42E) of Recombinant Horseradish Peroxidase C (Hrp C). within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe350

b:10.0
occ:1.00
 FE A:HEM350 0.0 10.0 1.0
NC A:HEM350 2.0 8.7 1.0
ND A:HEM350 2.0 10.1 1.0
NA A:HEM350 2.0 10.3 1.0
NB A:HEM350 2.0 9.7 1.0
NE2 A:HIS170 2.2 10.8 1.0
C1C A:HEM350 3.0 8.7 1.0
C4B A:HEM350 3.1 8.8 1.0
C1D A:HEM350 3.1 9.1 1.0
C4C A:HEM350 3.1 9.4 1.0
C4A A:HEM350 3.1 12.2 1.0
C4D A:HEM350 3.1 9.9 1.0
C1B A:HEM350 3.1 8.1 1.0
C1A A:HEM350 3.1 10.5 1.0
CE1 A:HIS170 3.2 11.9 1.0
CD2 A:HIS170 3.2 10.6 1.0
CHC A:HEM350 3.4 8.5 1.0
CHD A:HEM350 3.4 8.3 1.0
CHB A:HEM350 3.4 10.8 1.0
CHA A:HEM350 3.4 9.4 1.0
C2D A:HEM350 4.3 9.4 1.0
C3D A:HEM350 4.3 8.3 1.0
C2B A:HEM350 4.3 8.5 1.0
C2C A:HEM350 4.3 7.8 1.0
C3B A:HEM350 4.3 8.0 1.0
C3A A:HEM350 4.3 12.2 1.0
C2A A:HEM350 4.3 11.9 1.0
C3C A:HEM350 4.3 10.1 1.0
ND1 A:HIS170 4.4 12.3 1.0
CG A:HIS170 4.4 8.9 1.0
CE2 A:PHE41 4.7 17.9 1.0
CZ A:PHE221 4.7 11.2 1.0
CD2 A:PHE41 4.9 14.9 1.0
O A:HOH4057 5.0 32.8 1.0

Reference:

K.Meno, S.Jennings, A.T.Smith, A.Henriksen, M.Gajhede. Structural Analysis of the Two Horseradish Peroxidase Catalytic Residue Variants H42E and R38S/H42E: Implications For the Catalytic Cycle. Acta Crystallogr.,Sect.D V. 58 1803 2002.
ISSN: ISSN 0907-4449
PubMed: 12351824
DOI: 10.1107/S090744490201329X
Page generated: Sun Dec 13 14:21:30 2020

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