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Arsenic in PDB 3fkg: 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: 3fkg 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) 32.90 / 1.81
Space group P 43
Cell size a, b, c (Å), α, β, γ (°) 62.683, 62.683, 98.217, 90.00, 90.00, 90.00
R / Rfree (%) 15.2 / 20.1

Other elements in 3fkg:

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

Iron (Fe) 4 atoms
Calcium (Ca) 2 atoms
Zinc (Zn) 7 atoms

Arsenic Binding Sites:

The binding sites of Arsenic atom in the Crystal Structure Analysis of Fungal Versatile Peroxidase From Pleurotus Eryngii (pdb code 3fkg). This binding sites where shown within 5.0 Angstroms radius around Arsenic atom.
In total 2 binding sites of Arsenic where determined in the Crystal Structure Analysis of Fungal Versatile Peroxidase From Pleurotus Eryngii, PDB code: 3fkg:
Jump to Arsenic binding site number: 1; 2;

Arsenic binding site 1 out of 2 in 3fkg

Go back to Arsenic Binding Sites List in 3fkg
Arsenic binding site 1 out of 2 in the Crystal Structure Analysis of Fungal Versatile Peroxidase From Pleurotus Eryngii


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As 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:As342

b:17.5
occ:0.50
AS A:CAC342 0.0 17.5 0.5
O2 A:CAC342 1.7 21.2 0.5
O1 A:CAC342 1.7 19.6 0.5
C1 A:CAC342 1.9 19.5 0.5
C2 A:CAC342 2.0 19.6 0.5
ZN A:ZN334 3.2 15.3 0.5
ZN A:ZN338 3.3 27.3 0.6
O A:HIS136 3.6 23.3 1.0
O A:HOH418 3.9 37.9 1.0
OE1 A:GLU140 3.9 28.4 1.0
O A:HOH461 4.0 29.6 1.0
OD2 A:ASP143 4.0 21.4 1.0
C2 A:CAC343 4.1 23.5 0.4
C A:HIS136 4.2 22.5 1.0
CA A:HIS136 4.4 22.9 1.0
CB A:HIS136 4.4 26.7 1.0
O1 A:CAC343 4.4 33.4 0.4
O A:HOH561 4.5 23.7 1.0
O2 A:CAC343 4.5 24.3 0.4
O A:HOH413 4.6 48.0 0.6
AS A:CAC343 4.6 27.6 0.4
OD1 A:ASP143 4.6 24.3 1.0
CG A:ASP143 4.7 21.3 1.0
O A:VAL138 4.7 17.4 1.0
ND1 A:HIS136 4.8 30.8 1.0
CD A:GLU140 4.8 24.1 1.0
OG A:SER147 4.9 26.4 1.0

Arsenic binding site 2 out of 2 in 3fkg

Go back to Arsenic Binding Sites List in 3fkg
Arsenic binding site 2 out of 2 in the Crystal Structure Analysis of Fungal Versatile Peroxidase From Pleurotus Eryngii


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 2 of Crystal Structure Analysis of Fungal Versatile Peroxidase From Pleurotus Eryngii within 5.0Å range:
probe atom residue distance (Å) B Occ
A:As343

b:27.6
occ:0.40
AS A:CAC343 0.0 27.6 0.4
O1 A:CAC343 1.7 33.4 0.4
O2 A:CAC343 1.7 24.3 0.4
C2 A:CAC343 2.0 23.5 0.4
C1 A:CAC343 2.0 30.1 0.4
ZN A:ZN334 3.2 15.3 0.5
ZN A:ZN338 3.2 27.3 0.6
OE1 A:GLU140 3.4 28.4 1.0
O1 A:CAC342 3.7 19.6 0.5
O A:HOH374 3.9 37.2 0.5
O A:HOH484 4.0 32.8 0.5
O A:HOH413 4.1 48.0 0.6
O A:HOH663 4.2 48.2 1.0
O2 A:CAC342 4.3 21.2 0.5
CE1 A:PHE142 4.5 22.0 1.0
CD A:GLU140 4.5 24.1 1.0
AS A:CAC342 4.6 17.5 0.5
OD1 A:ASP143 4.6 24.3 1.0
O A:HOH418 4.7 37.9 1.0
OE2 A:GLU140 4.7 23.4 1.0
ND1 A:HIS136 4.8 30.8 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 Oct 27 16:50:06 2020

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