Iron in PDB 4atj: Distal Heme Pocket Mutant (H42E) of Recombinant Horseradish Peroxidase in Complex with Benzhydroxamic Acid

All present enzymatic activity of Distal Heme Pocket Mutant (H42E) of Recombinant Horseradish Peroxidase in Complex with Benzhydroxamic Acid:
1.11.1.7;

The structure of Distal Heme Pocket Mutant (H42E) of Recombinant Horseradish Peroxidase in Complex with Benzhydroxamic Acid, PDB code: 4atj was solved by K.Meno, S.Jennings, A.T.Smith, A.Henriksen, M.Gajhede, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.00 / 2.50
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	74.930, 62.270, 78.230, 90.00, 104.27, 90.00
R / Rfree (%)	16.2 / 19.4

The structure of Distal Heme Pocket Mutant (H42E) of Recombinant Horseradish Peroxidase in Complex with Benzhydroxamic Acid also contains other interesting chemical elements:

Calcium

(Ca)

4 atoms

The binding sites of Iron atom in the Distal Heme Pocket Mutant (H42E) of Recombinant Horseradish Peroxidase in Complex with Benzhydroxamic Acid (pdb code 4atj). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Distal Heme Pocket Mutant (H42E) of Recombinant Horseradish Peroxidase in Complex with Benzhydroxamic Acid, PDB code: 4atj:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Distal Heme Pocket Mutant (H42E) of Recombinant Horseradish Peroxidase in Complex with Benzhydroxamic Acid


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 (H42E) of Recombinant Horseradish Peroxidase in Complex with Benzhydroxamic Acid within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe350 b:10.2 occ:1.00 FE A:HEM350 0.0 10.2 1.0 NC A:HEM350 2.0 10.2 1.0 NB A:HEM350 2.0 11.0 1.0 NA A:HEM350 2.0 10.7 1.0 ND A:HEM350 2.0 10.3 1.0 NE2 A:HIS170 2.2 6.2 1.0 O A:HOH365 2.9 10.1 1.0 C1C A:HEM350 3.0 11.4 1.0 C4B A:HEM350 3.1 11.6 1.0 C1A A:HEM350 3.1 6.6 1.0 C4D A:HEM350 3.1 9.1 1.0 C1B A:HEM350 3.1 9.2 1.0 C4C A:HEM350 3.1 8.2 1.0 C4A A:HEM350 3.1 10.7 1.0 C1D A:HEM350 3.1 8.2 1.0 CE1 A:HIS170 3.2 11.3 1.0 CD2 A:HIS170 3.2 6.0 1.0 CHC A:HEM350 3.4 11.1 1.0 CHA A:HEM350 3.4 6.0 1.0 CHB A:HEM350 3.5 11.1 1.0 CHD A:HEM350 3.5 7.0 1.0 C2C A:HEM350 4.3 12.8 1.0 C3C A:HEM350 4.3 11.6 1.0 C2B A:HEM350 4.3 11.9 1.0 C2A A:HEM350 4.3 8.6 1.0 C3B A:HEM350 4.3 11.5 1.0 C3A A:HEM350 4.3 10.7 1.0 C3D A:HEM350 4.3 9.8 1.0 C2D A:HEM350 4.3 9.1 1.0 CG A:HIS170 4.4 10.6 1.0 ND1 A:HIS170 4.4 12.4 1.0 O1 A:BHO353 4.4 14.0 1.0 NE A:ARG38 4.6 18.0 1.0 CZ A:PHE221 4.9 9.5 1.0

Iron binding site 2 out of 2 in the Distal Heme Pocket Mutant (H42E) of Recombinant Horseradish Peroxidase in Complex with Benzhydroxamic Acid


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Distal Heme Pocket Mutant (H42E) of Recombinant Horseradish Peroxidase in Complex with Benzhydroxamic Acid within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe350 b:10.2 occ:1.00 FE B:HEM350 0.0 10.2 1.0 NC B:HEM350 2.0 10.2 1.0 NB B:HEM350 2.0 11.0 1.0 NA B:HEM350 2.0 10.7 1.0 ND B:HEM350 2.0 10.3 1.0 NE2 B:HIS170 2.2 6.2 1.0 O B:HOH364 2.9 10.1 1.0 C1C B:HEM350 3.0 11.4 1.0 C1A B:HEM350 3.1 6.6 1.0 C4B B:HEM350 3.1 11.6 1.0 C4D B:HEM350 3.1 9.1 1.0 C1B B:HEM350 3.1 9.2 1.0 C4C B:HEM350 3.1 8.2 1.0 C4A B:HEM350 3.1 10.7 1.0 C1D B:HEM350 3.1 8.2 1.0 CE1 B:HIS170 3.2 11.3 1.0 CD2 B:HIS170 3.2 6.0 1.0 CHC B:HEM350 3.4 11.1 1.0 CHA B:HEM350 3.4 6.0 1.0 CHB B:HEM350 3.5 11.1 1.0 CHD B:HEM350 3.5 7.0 1.0 C2C B:HEM350 4.3 12.8 1.0 C3C B:HEM350 4.3 11.6 1.0 C2B B:HEM350 4.3 11.9 1.0 C2A B:HEM350 4.3 8.6 1.0 C3B B:HEM350 4.3 11.5 1.0 C3A B:HEM350 4.3 10.7 1.0 C3D B:HEM350 4.3 9.8 1.0 C2D B:HEM350 4.3 9.1 1.0 CG B:HIS170 4.4 10.6 1.0 ND1 B:HIS170 4.4 12.4 1.0 O1 B:BHO353 4.4 14.0 1.0 NE B:ARG38 4.6 18.0 1.0 CZ B:PHE221 4.9 9.5 1.0

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