Iron in PDB 3atj: Heme Ligand Mutant of Recombinant Horseradish Peroxidase in Complex with Benzhydroxamic Acid

All present enzymatic activity of Heme Ligand Mutant of Recombinant Horseradish Peroxidase in Complex with Benzhydroxamic Acid:
1.11.1.7;

The structure of Heme Ligand Mutant of Recombinant Horseradish Peroxidase in Complex with Benzhydroxamic Acid, PDB code: 3atj was solved by K.Meno, C.G.White, A.T.Smith, M.Gajhede, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.20
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	75.105, 62.283, 78.160, 90.00, 104.31, 90.00
R / Rfree (%)	17.4 / 20.3

The structure of Heme Ligand Mutant 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 Heme Ligand Mutant of Recombinant Horseradish Peroxidase in Complex with Benzhydroxamic Acid (pdb code 3atj). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Heme Ligand Mutant of Recombinant Horseradish Peroxidase in Complex with Benzhydroxamic Acid, PDB code: 3atj:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Heme Ligand Mutant 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 Heme Ligand Mutant of Recombinant Horseradish Peroxidase in Complex with Benzhydroxamic Acid within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe350 b:12.1 occ:1.00 FE A:HEM350 0.0 12.1 1.0 NC A:HEM350 2.0 10.2 1.0 NA A:HEM350 2.0 11.8 1.0 NB A:HEM350 2.0 10.7 1.0 ND A:HEM350 2.0 11.3 1.0 NE2 A:HIS170 2.2 6.1 1.0 O A:HOH711 2.8 7.3 1.0 C1C A:HEM350 3.0 7.0 1.0 C4B A:HEM350 3.0 8.2 1.0 C1A A:HEM350 3.0 8.7 1.0 C4C A:HEM350 3.1 8.2 1.0 C4A A:HEM350 3.1 11.9 1.0 C1B A:HEM350 3.1 8.6 1.0 C4D A:HEM350 3.1 9.1 1.0 C1D A:HEM350 3.1 7.6 1.0 CE1 A:HIS170 3.1 5.3 1.0 CD2 A:HIS170 3.2 5.8 1.0 CHC A:HEM350 3.4 7.2 1.0 CHA A:HEM350 3.4 5.4 1.0 CHB A:HEM350 3.5 9.0 1.0 CHD A:HEM350 3.5 7.3 1.0 C2C A:HEM350 4.3 7.6 1.0 C2A A:HEM350 4.3 10.9 1.0 C3B A:HEM350 4.3 12.1 1.0 C3C A:HEM350 4.3 8.8 1.0 C2B A:HEM350 4.3 9.9 1.0 C3A A:HEM350 4.3 6.3 1.0 ND1 A:HIS170 4.3 7.6 1.0 C3D A:HEM350 4.3 11.8 1.0 C2D A:HEM350 4.3 9.4 1.0 CG A:HIS170 4.3 6.6 1.0 O1 A:BHO353 4.3 6.8 1.0 NE A:ARG38 4.6 8.4 1.0 CE2 A:PHE41 4.9 5.6 1.0 CE A:MET221 4.9 14.9 1.0 O2 A:BHO353 4.9 8.3 1.0

Iron binding site 2 out of 2 in the Heme Ligand Mutant 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 Heme Ligand Mutant of Recombinant Horseradish Peroxidase in Complex with Benzhydroxamic Acid within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe350 b:12.1 occ:1.00 FE B:HEM350 0.0 12.1 1.0 NC B:HEM350 2.0 10.2 1.0 NA B:HEM350 2.0 11.8 1.0 NB B:HEM350 2.0 10.7 1.0 ND B:HEM350 2.0 11.3 1.0 NE2 B:HIS170 2.2 6.1 1.0 O B:HOH1711 2.8 7.3 1.0 C1C B:HEM350 3.0 7.0 1.0 C4B B:HEM350 3.0 8.2 1.0 C1A B:HEM350 3.0 8.7 1.0 C4C B:HEM350 3.1 8.2 1.0 C4A B:HEM350 3.1 11.9 1.0 C1B B:HEM350 3.1 8.6 1.0 C4D B:HEM350 3.1 9.1 1.0 C1D B:HEM350 3.1 7.6 1.0 CE1 B:HIS170 3.1 5.3 1.0 CD2 B:HIS170 3.2 5.8 1.0 CHC B:HEM350 3.4 7.2 1.0 CHA B:HEM350 3.4 5.4 1.0 CHB B:HEM350 3.5 9.0 1.0 CHD B:HEM350 3.5 7.3 1.0 C2C B:HEM350 4.3 7.6 1.0 C3B B:HEM350 4.3 12.1 1.0 C2A B:HEM350 4.3 10.9 1.0 C3C B:HEM350 4.3 8.8 1.0 C2B B:HEM350 4.3 9.9 1.0 C3A B:HEM350 4.3 6.3 1.0 ND1 B:HIS170 4.3 7.6 1.0 C3D B:HEM350 4.3 11.8 1.0 C2D B:HEM350 4.3 9.4 1.0 CG B:HIS170 4.3 6.6 1.0 O1 B:BHO354 4.3 6.8 1.0 NE B:ARG38 4.6 8.4 1.0 CE2 B:PHE41 4.9 5.6 1.0 CE B:MET221 4.9 14.9 1.0 O2 B:BHO354 4.9 8.3 1.0

K.Meno, C.G.White, A.T.Smith, M.Gajhede. Structural and Catalytical Implications of A F221M Mutation in the Proximal Pocket of Horseradish Peroxidase C (Hrp C) To Be Published.