Iron in PDB 4blz: Crystal Structure of Fungal Versatile Peroxidase I From Pleurotus Ostreatus - Crystal Form VI

All present enzymatic activity of Crystal Structure of Fungal Versatile Peroxidase I From Pleurotus Ostreatus - Crystal Form VI:
1.11.1.16;

The structure of Crystal Structure of Fungal Versatile Peroxidase I From Pleurotus Ostreatus - Crystal Form VI, PDB code: 4blz was solved by F.J.Medrano, A.Romero, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.085 / 2.00
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	94.540, 38.620, 98.190, 90.00, 91.15, 90.00
R / Rfree (%)	22.31 / 27.18

The structure of Crystal Structure of Fungal Versatile Peroxidase I From Pleurotus Ostreatus - Crystal Form VI also contains other interesting chemical elements:

Calcium

(Ca)

4 atoms

The binding sites of Iron atom in the Crystal Structure of Fungal Versatile Peroxidase I From Pleurotus Ostreatus - Crystal Form VI (pdb code 4blz). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of Fungal Versatile Peroxidase I From Pleurotus Ostreatus - Crystal Form VI, PDB code: 4blz:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of Fungal Versatile Peroxidase I From Pleurotus Ostreatus - Crystal Form VI


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of Fungal Versatile Peroxidase I From Pleurotus Ostreatus - Crystal Form VI within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe500 b:15.6 occ:1.00 FE A:HEM500 0.0 15.6 1.0 NC A:HEM500 2.0 13.6 1.0 NB A:HEM500 2.1 16.7 1.0 NA A:HEM500 2.1 16.0 1.0 ND A:HEM500 2.1 15.8 1.0 NE2 A:HIS170 2.4 14.7 1.0 C1C A:HEM500 3.0 14.7 1.0 C4C A:HEM500 3.0 14.7 1.0 C1D A:HEM500 3.1 15.3 1.0 C4B A:HEM500 3.1 16.4 1.0 C4A A:HEM500 3.1 15.9 1.0 C1B A:HEM500 3.1 16.1 1.0 C1A A:HEM500 3.1 16.7 1.0 C4D A:HEM500 3.1 16.2 1.0 O A:HOH2066 3.1 36.9 1.0 CD2 A:HIS170 3.3 13.9 1.0 CHC A:HEM500 3.4 15.8 1.0 CE1 A:HIS170 3.4 11.9 1.0 CHD A:HEM500 3.4 14.7 1.0 CHB A:HEM500 3.5 15.1 1.0 CHA A:HEM500 3.5 16.2 1.0 C2C A:HEM500 4.2 14.2 1.0 C3C A:HEM500 4.3 13.8 1.0 C2D A:HEM500 4.3 15.9 1.0 C3B A:HEM500 4.3 16.8 1.0 C2B A:HEM500 4.3 15.8 1.0 C3D A:HEM500 4.3 16.2 1.0 C3A A:HEM500 4.3 16.0 1.0 C2A A:HEM500 4.3 17.2 1.0 CG A:HIS170 4.5 12.6 1.0 ND1 A:HIS170 4.5 12.1 1.0

Iron binding site 2 out of 2 in the Crystal Structure of Fungal Versatile Peroxidase I From Pleurotus Ostreatus - Crystal Form VI


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of Fungal Versatile Peroxidase I From Pleurotus Ostreatus - Crystal Form VI within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe500 b:16.2 occ:1.00 FE B:HEM500 0.0 16.2 1.0 NC B:HEM500 2.0 14.8 1.0 NB B:HEM500 2.1 14.7 1.0 NA B:HEM500 2.1 14.9 1.0 ND B:HEM500 2.1 17.6 1.0 NE2 B:HIS170 2.4 11.8 1.0 C1C B:HEM500 3.0 14.6 1.0 C4C B:HEM500 3.1 15.2 1.0 C4B B:HEM500 3.1 14.9 1.0 C1D B:HEM500 3.1 16.6 1.0 C1B B:HEM500 3.1 15.3 1.0 C4A B:HEM500 3.1 14.8 1.0 C4D B:HEM500 3.1 17.0 1.0 C1A B:HEM500 3.2 16.1 1.0 CD2 B:HIS170 3.3 11.6 1.0 O B:HOH2062 3.4 33.9 1.0 CHC B:HEM500 3.4 14.8 1.0 CHD B:HEM500 3.4 15.6 1.0 CE1 B:HIS170 3.4 12.1 1.0 CHB B:HEM500 3.5 15.0 1.0 CHA B:HEM500 3.5 16.9 1.0 C2C B:HEM500 4.3 15.2 1.0 C3C B:HEM500 4.3 15.1 1.0 C3B B:HEM500 4.3 15.4 1.0 C2B B:HEM500 4.3 15.4 1.0 C2D B:HEM500 4.3 17.0 1.0 C3A B:HEM500 4.4 16.0 1.0 C3D B:HEM500 4.4 17.6 1.0 C2A B:HEM500 4.4 16.8 1.0 CG B:HIS170 4.5 12.1 1.0 ND1 B:HIS170 4.5 12.7 1.0

E.Fernandez-Fueyo, F.J.Ruiz-Duenas, M.J.Martinez, A.Romero, K.E.Hammel, F.J.Medrano, A.T.Martinez. Ligninolytic Peroxidase Genes in the Oyster Mushroom Genome: Heterologous Expression, Molecular Structure, Catalytic and Stability Properties, and Lignin-Degrading Ability. Biotechnol.Biofuels V. 7 2 2014.
ISSN: ISSN 1754-6834
PubMed: 24387130
DOI: 10.1186/1754-6834-7-2