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Manganese in PDB 3fm1: Crystal Structure Analysis of Fungal Versatile Peroxidase From Pleurotus Eryngii

Enzymatic activity of Crystal Structure Analysis of Fungal Versatile Peroxidase From Pleurotus Eryngii

All present enzymatic activity of Crystal Structure Analysis of Fungal Versatile Peroxidase From Pleurotus Eryngii:
1.11.1.16;

Protein crystallography data

The structure of Crystal Structure Analysis of Fungal Versatile Peroxidase From Pleurotus Eryngii, PDB code: 3fm1 was solved by K.Piontek, A.T.Martinez, T.Choinowski, D.A.Plattner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.71 / 1.78
Space group P 43
Cell size a, b, c (Å), α, β, γ (°) 63.645, 63.645, 99.598, 90.00, 90.00, 90.00
R / Rfree (%) 12.4 / 17.2

Other elements in 3fm1:

The structure of Crystal Structure Analysis of Fungal Versatile Peroxidase From Pleurotus Eryngii also contains other interesting chemical elements:

Zinc (Zn) 3 atoms
Iron (Fe) 4 atoms
Calcium (Ca) 2 atoms
Sodium (Na) 5 atoms

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure Analysis of Fungal Versatile Peroxidase From Pleurotus Eryngii (pdb code 3fm1). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Crystal Structure Analysis of Fungal Versatile Peroxidase From Pleurotus Eryngii, PDB code: 3fm1:

Manganese binding site 1 out of 1 in 3fm1

Go back to Manganese Binding Sites List in 3fm1
Manganese binding site 1 out of 1 in the Crystal Structure Analysis of Fungal Versatile Peroxidase From Pleurotus Eryngii


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure Analysis of Fungal Versatile Peroxidase From Pleurotus Eryngii within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn353

b:24.8
occ:0.50
 O A:HOH1158 2.1 10.7 0.4
O1D A:HEM350 2.1 23.6 1.0
OE2 A:GLU36 2.1 16.6 0.4
OE2 A:GLU40 2.2 24.7 0.4
OD2 A:ASP175 2.2 17.8 0.4
O A:HOH1159 2.4 20.4 0.4
CGD A:HEM350 3.1 16.6 1.0
CD A:GLU36 3.1 16.5 0.4
CD A:GLU40 3.1 20.5 0.4
O A:HOH1160 3.2 25.8 0.6
OD2 A:ASP175 3.2 20.5 0.6
CG A:ASP175 3.2 15.0 0.4
O A:HOH1166 3.3 22.6 0.5
OE1 A:GLU36 3.3 20.4 0.4
CG A:ASP175 3.5 16.1 0.6
O2D A:HEM350 3.5 13.3 1.0
OD1 A:ASP175 3.5 15.2 0.6
CG A:GLU40 3.6 13.1 0.4
OD1 A:ASP175 3.6 15.3 0.4
O A:HOH1163 3.9 20.6 0.5
CG A:GLU40 4.0 12.9 0.6
O A:HOH805 4.1 8.0 0.6
OE1 A:GLU40 4.2 26.0 0.4
FE A:FE336 4.2 19.6 0.6
O A:HOH1161 4.3 48.6 1.0
CBD A:HEM350 4.3 9.5 1.0
O A:ALA173 4.4 11.3 1.0
CG A:GLU36 4.4 12.1 0.4
CB A:ASP175 4.4 13.5 0.4
CB A:ASP175 4.5 13.2 0.6
CD A:GLU40 4.6 14.0 0.6
ZN A:ZN335 4.6 26.9 0.3
O A:HOH1176 4.8 42.9 1.0
OE2 A:GLU40 4.9 11.2 0.6
O2A A:HEM350 4.9 15.1 1.0
C A:ALA173 4.9 10.7 1.0
N A:ASP175 4.9 10.9 1.0

Reference:

K.Piontek, T.Choinowski, M.Perez-Boada, F.J.Ruiz-Duenas, M.J.Martinez, D.A.Plattner, A.T.Martinez. Structural and Site-Directed Mutagenesis Study of Versatile Peroxidase Oxidizing Both Mn(II) and Aromatic Substrates To Be Published.
Page generated: Tue Dec 15 04:09:38 2020

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