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Arsenic in PDB 3fmu: 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: 3fmu 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) 44.69 / 1.04
Space group P 43
Cell size a, b, c (Å), α, β, γ (°) 63.199, 63.199, 99.237, 90.00, 90.00, 90.00
R / Rfree (%) 11.1 / 12.3

Other elements in 3fmu:

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

Zinc (Zn) 8 atoms
Iron (Fe) 6 atoms
Calcium (Ca) 2 atoms

Arsenic Binding Sites:

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

Arsenic binding site 1 out of 1 in 3fmu

Go back to Arsenic Binding Sites List in 3fmu
Arsenic 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 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:As345

b:13.7
occ:0.50
 AS A:CAC345 0.0 13.7 0.5
O1 A:CAC345 1.7 13.4 0.5
O2 A:CAC345 1.7 18.2 0.5
C2 A:CAC345 2.0 19.1 0.5
C1 A:CAC345 2.0 11.4 0.5
O A:HOH660 2.6 9.8 0.5
ZN A:ZN338 3.2 23.0 0.6
ZN A:ZN334 3.3 12.2 0.5
O A:HOH776 3.4 12.8 0.5
O A:HIS136 3.7 11.6 1.0
HB3 A:HIS136 3.7 15.1 1.0
O A:HOH626 3.7 26.4 0.6
O A:HOH861 3.8 25.4 0.5
O A:HOH370 4.0 23.5 1.0
O A:HOH567 4.0 24.4 0.5
HA A:HIS136 4.0 11.1 1.0
OD2 A:ASP143 4.1 9.6 1.0
O A:HOH627 4.2 13.8 0.5
O A:HOH638 4.2 15.8 0.5
C A:HIS136 4.3 8.8 1.0
O A:HOH393 4.3 12.1 1.0
O A:HOH625 4.4 14.9 0.6
CB A:HIS136 4.5 15.1 1.0
CA A:HIS136 4.5 11.0 1.0
HA A:PRO139 4.7 7.5 1.0
O A:VAL138 4.7 7.3 1.0
CG A:ASP143 4.7 8.8 1.0
OD1 A:ASP143 4.7 11.3 1.0
OG A:SER147 4.8 11.2 1.0
ND1 A:HIS136 4.9 23.5 1.0
HG3 A:GLU140 4.9 13.3 1.0
HD2 A:ARG151 4.9 6.9 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: Wed Jul 10 11:40:06 2024

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