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Iron in PDB 4bm3: Crystal Structure of Manganese Peroxidase 4 From Pleurotus Ostreatus - Crystal Form III

Enzymatic activity of Crystal Structure of Manganese Peroxidase 4 From Pleurotus Ostreatus - Crystal Form III

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

Protein crystallography data

The structure of Crystal Structure of Manganese Peroxidase 4 From Pleurotus Ostreatus - Crystal Form III, PDB code: 4bm3 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) 38.366 / 1.65
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 124.250, 86.530, 40.300, 90.00, 107.82, 90.00
R / Rfree (%) 21.04 / 24.22

Other elements in 4bm3:

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

Calcium (Ca) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Manganese Peroxidase 4 From Pleurotus Ostreatus - Crystal Form III (pdb code 4bm3). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Crystal Structure of Manganese Peroxidase 4 From Pleurotus Ostreatus - Crystal Form III, PDB code: 4bm3:

Iron binding site 1 out of 1 in 4bm3

Go back to Iron Binding Sites List in 4bm3
Iron binding site 1 out of 1 in the Crystal Structure of Manganese Peroxidase 4 From Pleurotus Ostreatus - Crystal Form III


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 III within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe500

b:14.4
occ:1.00
 FE A:HEM500 0.0 14.4 1.0
NB A:HEM500 2.0 16.1 1.0
NA A:HEM500 2.0 13.3 1.0
NC A:HEM500 2.0 10.3 1.0
ND A:HEM500 2.1 14.6 1.0
NE2 A:HIS176 2.2 14.7 1.0
O A:HOH2078 2.5 29.0 1.0
C1B A:HEM500 3.0 18.9 1.0
C1C A:HEM500 3.0 14.3 1.0
C4A A:HEM500 3.0 14.9 1.0
C1A A:HEM500 3.0 15.0 1.0
C4C A:HEM500 3.1 12.7 1.0
C1D A:HEM500 3.1 12.0 1.0
CE1 A:HIS176 3.1 10.8 1.0
C4D A:HEM500 3.1 15.0 1.0
C4B A:HEM500 3.1 16.7 1.0
CD2 A:HIS176 3.3 14.3 1.0
CHB A:HEM500 3.4 19.2 1.0
CHA A:HEM500 3.5 15.2 1.0
CHD A:HEM500 3.5 15.2 1.0
CHC A:HEM500 3.5 16.0 1.0
C2C A:HEM500 4.2 12.7 1.0
C3C A:HEM500 4.2 10.7 1.0
C3A A:HEM500 4.2 13.7 1.0
ND1 A:HIS176 4.3 11.1 1.0
C2A A:HEM500 4.3 16.3 1.0
C2D A:HEM500 4.3 14.4 1.0
C2B A:HEM500 4.3 14.2 1.0
C3D A:HEM500 4.3 15.2 1.0
C3B A:HEM500 4.3 17.3 1.0
CG A:HIS176 4.4 12.9 1.0
CD2 A:LEU173 4.9 14.1 1.0
CG A:ARG44 4.9 15.9 1.0
CD A:ARG44 5.0 22.4 1.0
OG A:SER175 5.0 15.4 1.0

Reference:

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
Page generated: Mon Aug 5 00:07:16 2024

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