Arsenic in PDB 5dak: Crystal Structure of Human Glutathione Transferase Pi Complexed with A Metalloid in the Absence of Glutathione

All present enzymatic activity of Crystal Structure of Human Glutathione Transferase Pi Complexed with A Metalloid in the Absence of Glutathione:
2.5.1.18;

The structure of Crystal Structure of Human Glutathione Transferase Pi Complexed with A Metalloid in the Absence of Glutathione, PDB code: 5dak was solved by L.J.Parker, M.W.Parker, C.J.Morton, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.90 / 2.11
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	74.629, 95.509, 68.247, 90.00, 98.26, 90.00
R / Rfree (%)	15.7 / 20.4

The binding sites of Arsenic atom in the Crystal Structure of Human Glutathione Transferase Pi Complexed with A Metalloid in the Absence of Glutathione (pdb code 5dak). 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 of Human Glutathione Transferase Pi Complexed with A Metalloid in the Absence of Glutathione, PDB code: 5dak:
Jump to Arsenic binding site number: 1; 2;

Arsenic binding site 1 out of 2 in the Crystal Structure of Human Glutathione Transferase Pi Complexed with A Metalloid in the Absence of Glutathione


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of Crystal Structure of Human Glutathione Transferase Pi Complexed with A Metalloid in the Absence of Glutathione within 5.0Å range: probe atom residue distance (Å) B Occ A:As302 b:56.1 occ:0.30 HG A:CYS101 2.3 54.3 1.0 SG A:CYS101 2.4 45.3 1.0 HB3 A:CYS101 2.8 33.2 1.0 CB A:CYS101 3.2 27.7 1.0 HG3 A:LYS102 3.7 30.3 1.0 HB2 A:CYS101 3.8 33.2 1.0 C A:CYS101 4.0 20.5 1.0 HG2 A:LYS102 4.1 30.3 1.0 N A:LYS102 4.1 23.1 1.0 H A:LYS102 4.2 27.8 1.0 CA A:CYS101 4.2 23.3 1.0 O A:ASP98 4.2 20.4 1.0 CG A:LYS102 4.3 25.3 1.0 HA A:LYS102 4.4 24.2 1.0 O A:CYS101 4.5 24.2 1.0 HA A:ASP98 4.5 20.4 1.0 HE3 A:LYS102 4.7 38.2 1.0 CA A:LYS102 4.8 20.2 1.0 HA A:CYS101 4.8 28.0 1.0 HE2 A:LYS102 4.8 38.2 1.0 H A:CYS101 5.0 22.4 1.0

Arsenic binding site 2 out of 2 in the Crystal Structure of Human Glutathione Transferase Pi Complexed with A Metalloid in the Absence of Glutathione


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 2 of Crystal Structure of Human Glutathione Transferase Pi Complexed with A Metalloid in the Absence of Glutathione within 5.0Å range: probe atom residue distance (Å) B Occ B:As302 b:50.2 occ:0.30 HG B:CYS101 1.4 36.8 0.6 SG B:CYS101 2.3 30.6 0.6 HB3 B:CYS101 2.6 30.8 0.4 HB3 B:CYS101 3.0 31.1 0.6 CB B:CYS101 3.2 25.9 0.6 HB2 B:CYS101 3.3 30.8 0.4 CB B:CYS101 3.4 25.7 0.4 C B:CYS101 3.6 21.5 1.0 HA B:LYS102 3.6 33.3 1.0 HG2 B:LYS102 3.7 33.5 1.0 N B:LYS102 3.7 24.6 1.0 O B:CYS101 3.8 25.4 1.0 HG3 B:LYS102 3.8 33.5 1.0 H B:LYS102 3.9 29.5 1.0 HB2 B:CYS101 4.0 31.1 0.6 CA B:CYS101 4.0 22.8 0.6 CA B:CYS101 4.1 22.9 0.4 CA B:LYS102 4.2 27.7 1.0 CG B:LYS102 4.2 27.9 1.0 HB2 B:SER105 4.5 31.4 1.0 HA B:CYS101 4.5 27.3 0.6 HA B:CYS101 4.7 27.4 0.4 O B:ASP98 4.7 22.2 1.0 HB3 B:SER105 4.8 31.4 1.0 HG B:CYS101 4.8 40.6 0.4 SG B:CYS101 4.8 33.9 0.4 CB B:LYS102 4.8 27.8 1.0

L.J.Parker, M.W.Parker, C.J.Morton, A.Bocedi, D.B.Ascher, J.B.Aitken, H.H.Harris, M.Lo Bello, G.Ricci. Visualisation of Organoarsenic Human Glutathione Transferase P1-1 Complexes: Metabolism of Arsenic-Based Therapeutics To Be Published.