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Atomistry » Arsenic » PDB 4zt2-5hr7 » 5ag1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Arsenic » PDB 4zt2-5hr7 » 5ag1 » |
Arsenic in PDB 5ag1: Dyp-Type Peroxidase of Auricularia Auricula-Judae (Aaudypi) with Meso-Nitrated HemeEnzymatic activity of Dyp-Type Peroxidase of Auricularia Auricula-Judae (Aaudypi) with Meso-Nitrated Heme
All present enzymatic activity of Dyp-Type Peroxidase of Auricularia Auricula-Judae (Aaudypi) with Meso-Nitrated Heme:
1.11.1.19; Protein crystallography data
The structure of Dyp-Type Peroxidase of Auricularia Auricula-Judae (Aaudypi) with Meso-Nitrated Heme, PDB code: 5ag1
was solved by
E.Strittmatter,
K.Piontek,
D.A.Plattner,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5ag1:
The structure of Dyp-Type Peroxidase of Auricularia Auricula-Judae (Aaudypi) with Meso-Nitrated Heme also contains other interesting chemical elements:
Arsenic Binding Sites:
The binding sites of Arsenic atom in the Dyp-Type Peroxidase of Auricularia Auricula-Judae (Aaudypi) with Meso-Nitrated Heme
(pdb code 5ag1). This binding sites where shown within
5.0 Angstroms radius around Arsenic atom.
In total 2 binding sites of Arsenic where determined in the Dyp-Type Peroxidase of Auricularia Auricula-Judae (Aaudypi) with Meso-Nitrated Heme, PDB code: 5ag1: Jump to Arsenic binding site number: 1; 2; Arsenic binding site 1 out of 2 in 5ag1Go back to![]() ![]()
Arsenic binding site 1 out
of 2 in the Dyp-Type Peroxidase of Auricularia Auricula-Judae (Aaudypi) with Meso-Nitrated Heme
![]() Mono view ![]() Stereo pair view
Arsenic binding site 2 out of 2 in 5ag1Go back to![]() ![]()
Arsenic binding site 2 out
of 2 in the Dyp-Type Peroxidase of Auricularia Auricula-Judae (Aaudypi) with Meso-Nitrated Heme
![]() Mono view ![]() Stereo pair view
Reference:
E.Strittmatter,
K.Piontek,
D.A.Plattner.
Crystallographic Trapping of A Covalently Modified Heme in A Dye-Decolorizing Peroxidase To Be Published.
Page generated: Mon Jul 7 00:12:37 2025
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