Iron in PDB 3fm4: Crystal Structure Analysis of Fungal Versatile Peroxidase From Pleurotus Eryngii

All present enzymatic activity of Crystal Structure Analysis of Fungal Versatile Peroxidase From Pleurotus Eryngii:
1.11.1.16;

The structure of Crystal Structure Analysis of Fungal Versatile Peroxidase From Pleurotus Eryngii, PDB code: 3fm4 was solved by K.Piontek, A.T.Martinez, T.Choinowski, D.A.Plattner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	32.88 / 2.11
Space group	P 43
Cell size a, b, c (Å), α, β, γ (°)	62.794, 62.794, 97.875, 90.00, 90.00, 90.00
R / Rfree (%)	14.1 / 19.8

The structure of Crystal Structure Analysis of Fungal Versatile Peroxidase From Pleurotus Eryngii also contains other interesting chemical elements:

Arsenic	(As)	2 atoms
Calcium	(Ca)	2 atoms
Zinc	(Zn)	6 atoms

The binding sites of Iron atom in the Crystal Structure Analysis of Fungal Versatile Peroxidase From Pleurotus Eryngii (pdb code 3fm4). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 3 binding sites of Iron where determined in the Crystal Structure Analysis of Fungal Versatile Peroxidase From Pleurotus Eryngii, PDB code: 3fm4:
Jump to Iron binding site number: 1; 2; 3;

Iron binding site 1 out of 3 in the Crystal Structure Analysis of Fungal Versatile Peroxidase From Pleurotus Eryngii


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure Analysis of Fungal Versatile Peroxidase From Pleurotus Eryngii within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe350 b:19.3 occ:1.00 FE A:HEM350 0.0 19.3 1.0 NA A:HEM350 2.1 17.9 1.0 NC A:HEM350 2.1 20.5 1.0 NE2 A:HIS169 2.1 18.3 1.0 ND A:HEM350 2.1 21.5 1.0 NB A:HEM350 2.1 17.2 1.0 O A:HOH510 2.9 54.7 1.0 CE1 A:HIS169 3.0 15.9 1.0 C1D A:HEM350 3.1 21.5 1.0 C1A A:HEM350 3.1 19.6 1.0 C4C A:HEM350 3.1 18.3 1.0 C4D A:HEM350 3.1 22.2 1.0 C1C A:HEM350 3.1 18.7 1.0 C4B A:HEM350 3.1 18.8 1.0 C4A A:HEM350 3.1 18.9 1.0 C1B A:HEM350 3.2 16.4 1.0 CD2 A:HIS169 3.2 16.8 1.0 CHD A:HEM350 3.4 20.1 1.0 CHA A:HEM350 3.4 17.2 1.0 CHC A:HEM350 3.5 18.4 1.0 CHB A:HEM350 3.5 17.9 1.0 ND1 A:HIS169 4.2 14.3 1.0 C2D A:HEM350 4.3 19.2 1.0 CG A:HIS169 4.3 14.7 1.0 C2A A:HEM350 4.3 17.5 1.0 C3D A:HEM350 4.3 20.1 1.0 C3C A:HEM350 4.3 19.6 1.0 C3A A:HEM350 4.3 19.2 1.0 C2C A:HEM350 4.3 18.4 1.0 C3B A:HEM350 4.3 21.6 1.0 C2B A:HEM350 4.4 19.4 1.0 O A:HOH491 4.4 41.0 1.0 CD2 A:LEU166 4.8 17.9 1.0

Iron binding site 2 out of 3 in the Crystal Structure Analysis of Fungal Versatile Peroxidase From Pleurotus Eryngii


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure Analysis of Fungal Versatile Peroxidase From Pleurotus Eryngii within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe335 b:14.2 occ:0.30 NE2 A:HIS293 2.0 33.4 1.0 OD2 A:ASP318 2.0 43.3 1.0 O A:HOH647 2.2 53.0 1.0 CE1 A:HIS293 2.9 40.9 1.0 CG A:ASP318 2.9 51.8 1.0 CD2 A:HIS293 3.0 40.3 1.0 OD1 A:ASP318 3.2 54.1 1.0 O A:HOH379 4.0 33.9 1.0 ND1 A:HIS293 4.0 40.0 1.0 CG A:HIS293 4.1 39.6 1.0 CB A:ASP318 4.3 53.2 1.0 O A:HOH619 4.8 60.1 1.0

Iron binding site 3 out of 3 in the Crystal Structure Analysis of Fungal Versatile Peroxidase From Pleurotus Eryngii


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Crystal Structure Analysis of Fungal Versatile Peroxidase From Pleurotus Eryngii within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe339 b:33.0 occ:0.33 OD1 A:ASP69 2.1 33.6 1.0 O A:HOH447 2.3 45.1 1.0 O A:HOH366 2.4 22.4 0.3 O A:HOH583 2.6 37.0 1.0 CG A:ASP69 3.1 31.1 1.0 NZ A:LYS89 3.3 50.9 1.0 OD2 A:ASP69 3.5 35.4 1.0 O A:HOH368 3.9 57.9 1.0 OG1 A:THR70 4.0 38.6 1.0 O A:ALA67 4.3 24.1 1.0 O A:ILE66 4.4 20.9 1.0 N A:ASP69 4.4 25.1 1.0 CB A:ASP69 4.5 28.3 1.0 N A:THR70 4.5 27.2 1.0 CE A:LYS89 4.6 46.7 1.0 CA A:ASP69 4.9 26.3 1.0 C A:ALA67 4.9 25.3 1.0

K.Piontek, T.Choinowski, M.Perez-Boada, F.J.Ruiz-Duenas, M.J.Martinez, D.A.Plattner, A.T.Martinez. Structural and Site-Directed Mutagenesis Study of Versatile Peroxidase Oxidizing Both Mn(II) and Aromatic Substrates To Be Published.