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Iron in PDB 4bm0: Crystal Structure of Fungal Versatile Peroxidase I From Pleurotus Ostreatus - Crystal Form VII

Enzymatic activity of Crystal Structure of Fungal Versatile Peroxidase I From Pleurotus Ostreatus - Crystal Form VII

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

Protein crystallography data

The structure of Crystal Structure of Fungal Versatile Peroxidase I From Pleurotus Ostreatus - Crystal Form VII, PDB code: 4bm0 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) 48.350 / 2.20
Space group P 43
Cell size a, b, c (Å), α, β, γ (°) 96.700, 96.700, 38.400, 90.00, 90.00, 90.00
R / Rfree (%) 22.79 / 27.12

Other elements in 4bm0:

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

Calcium (Ca) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Fungal Versatile Peroxidase I From Pleurotus Ostreatus - Crystal Form VII (pdb code 4bm0). 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 Fungal Versatile Peroxidase I From Pleurotus Ostreatus - Crystal Form VII, PDB code: 4bm0:

Iron binding site 1 out of 1 in 4bm0

Go back to Iron Binding Sites List in 4bm0
Iron binding site 1 out of 1 in the Crystal Structure of Fungal Versatile Peroxidase I From Pleurotus Ostreatus - Crystal Form VII


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

b:31.9
occ:1.00
 FE A:HEM500 0.0 31.9 1.0
NC A:HEM500 2.0 31.8 1.0
NA A:HEM500 2.1 38.2 1.0
NB A:HEM500 2.1 28.1 1.0
ND A:HEM500 2.2 26.5 1.0
NE2 A:HIS170 2.4 15.6 1.0
C1C A:HEM500 3.0 27.5 1.0
C4B A:HEM500 3.1 30.8 1.0
C1A A:HEM500 3.1 35.0 1.0
C4C A:HEM500 3.1 32.5 1.0
C4A A:HEM500 3.1 35.8 1.0
C1B A:HEM500 3.1 30.8 1.0
C4D A:HEM500 3.2 32.2 1.0
C1D A:HEM500 3.2 24.3 1.0
CD2 A:HIS170 3.3 18.2 1.0
CHC A:HEM500 3.4 29.9 1.0
CHA A:HEM500 3.5 33.0 1.0
CE1 A:HIS170 3.5 15.7 1.0
CHD A:HEM500 3.5 28.9 1.0
CHB A:HEM500 3.5 34.4 1.0
C2C A:HEM500 4.2 27.1 1.0
C3C A:HEM500 4.3 30.6 1.0
C3B A:HEM500 4.3 32.7 1.0
C2A A:HEM500 4.3 34.1 1.0
C3A A:HEM500 4.3 34.2 1.0
C2B A:HEM500 4.3 27.7 1.0
C3D A:HEM500 4.4 32.5 1.0
C2D A:HEM500 4.4 26.7 1.0
CG A:HIS170 4.5 20.2 1.0
ND1 A:HIS170 4.6 16.3 1.0
CD2 A:PHE47 4.8 32.4 1.0
CD2 A:LEU167 4.9 28.0 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 00:06:39 2024

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