Iron in PDB 4bm1: Crystal Structure of Manganese Peroxidase 4 From Pleurotus Ostreatus - Crystal Form I

All present enzymatic activity of Crystal Structure of Manganese Peroxidase 4 From Pleurotus Ostreatus - Crystal Form I:
1.11.1.13;

The structure of Crystal Structure of Manganese Peroxidase 4 From Pleurotus Ostreatus - Crystal Form I, PDB code: 4bm1 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)	38.148 / 1.10
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	39.990, 75.370, 75.610, 69.75, 75.69, 75.82
R / Rfree (%)	13.12 / 14.73

The structure of Crystal Structure of Manganese Peroxidase 4 From Pleurotus Ostreatus - Crystal Form I also contains other interesting chemical elements:

Calcium

(Ca)

4 atoms

The binding sites of Iron atom in the Crystal Structure of Manganese Peroxidase 4 From Pleurotus Ostreatus - Crystal Form I (pdb code 4bm1). 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 Manganese Peroxidase 4 From Pleurotus Ostreatus - Crystal Form I, PDB code: 4bm1:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of Manganese Peroxidase 4 From Pleurotus Ostreatus - Crystal Form I


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 Manganese Peroxidase 4 From Pleurotus Ostreatus - Crystal Form I within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe500 b:7.0 occ:1.00 FE A:HEM500 0.0 7.0 1.0 ND A:HEM500 2.0 7.5 1.0 NB A:HEM500 2.0 7.5 1.0 NC A:HEM500 2.0 7.7 1.0 NA A:HEM500 2.0 6.7 1.0 NE2 A:HIS176 2.1 6.0 1.0 C1D A:HEM500 3.0 6.5 1.0 C1C A:HEM500 3.0 7.2 1.0 C1B A:HEM500 3.1 7.1 1.0 C4A A:HEM500 3.1 6.3 1.0 C4D A:HEM500 3.1 6.7 1.0 C4C A:HEM500 3.1 6.7 1.0 C4B A:HEM500 3.1 7.5 1.0 CE1 A:HIS176 3.1 6.0 1.0 C1A A:HEM500 3.1 6.7 1.0 CD2 A:HIS176 3.1 5.9 1.0 HE1 A:HIS176 3.2 7.2 1.0 HD2 A:HIS176 3.3 7.1 1.0 CHC A:HEM500 3.4 7.2 1.0 CHD A:HEM500 3.4 6.8 1.0 CHB A:HEM500 3.4 6.8 1.0 CHA A:HEM500 3.5 7.0 1.0 O A:HOH2120 3.6 27.6 1.0 ND1 A:HIS176 4.2 6.1 1.0 C3D A:HEM500 4.2 6.8 1.0 C2D A:HEM500 4.3 7.1 1.0 C3C A:HEM500 4.3 7.7 1.0 C2C A:HEM500 4.3 7.2 1.0 C2B A:HEM500 4.3 7.5 1.0 CG A:HIS176 4.3 5.6 1.0 C3B A:HEM500 4.3 7.5 1.0 HE2 A:PHE193 4.3 8.6 1.0 C3A A:HEM500 4.3 7.1 1.0 HD21 A:LEU173 4.3 8.1 1.0 C2A A:HEM500 4.3 6.8 1.0 HHC A:HEM500 4.4 8.6 1.0 HHD A:HEM500 4.4 8.1 1.0 HHB A:HEM500 4.4 8.1 1.0 HHA A:HEM500 4.4 8.4 1.0 HD22 A:LEU173 4.5 8.1 1.0 HD2 A:PHE47 4.6 12.2 1.0 CD2 A:LEU173 4.8 6.7 1.0 HE2 A:HIS48 4.8 13.2 1.0 HD12 A:LEU235 4.9 8.8 1.0 HD23 A:LEU173 4.9 8.1 1.0 OG A:SER175 5.0 6.8 1.0 CG A:ARG44 5.0 15.2 1.0 HD1 A:HIS176 5.0 7.3 1.0

Iron binding site 2 out of 2 in the Crystal Structure of Manganese Peroxidase 4 From Pleurotus Ostreatus - Crystal Form I


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 Manganese Peroxidase 4 From Pleurotus Ostreatus - Crystal Form I within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe500 b:6.9 occ:1.00 FE B:HEM500 0.0 6.9 1.0 NB B:HEM500 2.0 7.3 1.0 NC B:HEM500 2.0 7.1 1.0 ND B:HEM500 2.1 7.7 1.0 NA B:HEM500 2.1 6.6 1.0 NE2 B:HIS176 2.1 6.3 1.0 C1C B:HEM500 3.0 6.4 1.0 C1D B:HEM500 3.1 6.3 1.0 C4B B:HEM500 3.1 7.4 1.0 C4C B:HEM500 3.1 6.6 1.0 C4D B:HEM500 3.1 6.6 1.0 CE1 B:HIS176 3.1 5.9 1.0 C1B B:HEM500 3.1 6.6 1.0 C1A B:HEM500 3.1 6.7 1.0 C4A B:HEM500 3.1 6.3 1.0 CD2 B:HIS176 3.2 6.2 1.0 HE1 B:HIS176 3.2 7.0 1.0 HD2 B:HIS176 3.4 7.5 1.0 CHC B:HEM500 3.4 6.8 1.0 CHD B:HEM500 3.4 6.0 1.0 CHA B:HEM500 3.5 6.3 1.0 CHB B:HEM500 3.5 6.7 1.0 O B:HOH2098 3.6 22.0 1.0 HE B:ARG44 3.6 15.1 0.5 HG3 B:ARG44 4.1 12.3 1.0 ND1 B:HIS176 4.2 6.1 1.0 C2D B:HEM500 4.2 6.4 1.0 C3D B:HEM500 4.3 6.8 1.0 C2C B:HEM500 4.3 7.4 1.0 C3B B:HEM500 4.3 7.0 1.0 HD21 B:LEU173 4.3 8.4 1.0 C3C B:HEM500 4.3 7.3 1.0 CG B:HIS176 4.3 5.9 1.0 C2B B:HEM500 4.3 6.9 1.0 C3A B:HEM500 4.3 6.7 1.0 C2A B:HEM500 4.3 6.4 1.0 HE2 B:PHE193 4.3 9.6 1.0 HHC B:HEM500 4.4 8.2 1.0 HHA B:HEM500 4.4 7.6 1.0 HHD B:HEM500 4.4 7.2 1.0 HHB B:HEM500 4.4 8.1 1.0 NE B:ARG44 4.5 12.6 0.5 HD22 B:LEU173 4.5 8.4 1.0 HH21 B:ARG44 4.5 15.0 0.5 HD2 B:ARG44 4.6 14.0 0.5 HD2 B:PHE47 4.6 13.2 1.0 CD2 B:LEU173 4.8 7.0 1.0 HE B:ARG44 4.8 14.7 0.5 HE2 B:HIS48 4.8 12.9 1.0 HD12 B:LEU235 4.9 8.7 1.0 HE2 B:PHE47 4.9 14.0 1.0 HD23 B:LEU173 4.9 8.4 1.0 OG B:SER175 5.0 6.8 1.0 HD1 B:HIS176 5.0 7.3 1.0 CG B:ARG44 5.0 10.3 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