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

Enzymatic activity of 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;

Protein crystallography data

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

Other elements in 4blz:

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

Iron Binding Sites:

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 4blz

Go back to Iron Binding Sites List in 4blz
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 4blz

Go back to Iron Binding Sites List in 4blz
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

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: Sun Dec 13 15:29:10 2020

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