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Arsenic in PDB 5ddl: Crystal Structure of Wt Human Glutathione Transferase Pi Soaked with A Metalloid Then Back-Soaked with Glutathione

Enzymatic activity of Crystal Structure of Wt Human Glutathione Transferase Pi Soaked with A Metalloid Then Back-Soaked with Glutathione

All present enzymatic activity of Crystal Structure of Wt Human Glutathione Transferase Pi Soaked with A Metalloid Then Back-Soaked with Glutathione:
2.5.1.18;

Protein crystallography data

The structure of Crystal Structure of Wt Human Glutathione Transferase Pi Soaked with A Metalloid Then Back-Soaked with Glutathione, PDB code: 5ddl 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) 37.50 / 1.98
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 77.665, 89.795, 68.854, 90.00, 98.08, 90.00
R / Rfree (%) 13.8 / 17.8

Other elements in 5ddl:

The structure of Crystal Structure of Wt Human Glutathione Transferase Pi Soaked with A Metalloid Then Back-Soaked with Glutathione also contains other interesting chemical elements:

Calcium (Ca) 2 atoms

Arsenic Binding Sites:

The binding sites of Arsenic atom in the Crystal Structure of Wt Human Glutathione Transferase Pi Soaked with A Metalloid Then Back-Soaked with Glutathione (pdb code 5ddl). 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 Wt Human Glutathione Transferase Pi Soaked with A Metalloid Then Back-Soaked with Glutathione, PDB code: 5ddl:
Jump to Arsenic binding site number: 1; 2;

Arsenic binding site 1 out of 2 in 5ddl

Go back to Arsenic Binding Sites List in 5ddl
Arsenic binding site 1 out of 2 in the Crystal Structure of Wt Human Glutathione Transferase Pi Soaked with A Metalloid Then Back-Soaked with 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 Wt Human Glutathione Transferase Pi Soaked with A Metalloid Then Back-Soaked with Glutathione within 5.0Å range:
probe atom residue distance (Å) B Occ
A:As302

b:48.0
occ:0.60
AS1 A:5AU302 0.0 48.0 0.6
C32 A:5AU302 2.1 28.3 0.6
HB22 A:GSH303 2.3 23.2 0.4
S12 A:5AU302 2.4 46.4 0.6
S10 A:5AU302 2.4 32.3 0.6
C37 A:5AU302 3.0 25.2 0.6
C33 A:5AU302 3.0 34.3 0.6
OH A:TYR108 3.2 16.6 1.0
CB2 A:GSH303 3.3 19.3 0.4
HH A:TYR108 3.3 19.9 1.0
HSG A:GSH303 3.4 20.2 0.4
C13 A:5AU302 3.4 15.3 0.6
CZ A:TYR108 3.5 15.8 1.0
C09 A:5AU302 3.6 26.1 0.6
HB23 A:GSH303 3.7 23.2 0.4
SG2 A:GSH303 3.9 16.8 0.4
HA2 A:GSH303 4.0 21.1 0.4
CE2 A:TYR108 4.1 15.5 1.0
CE1 A:TYR108 4.1 18.6 1.0
HE2 A:TYR108 4.1 18.6 1.0
HE1 A:TYR108 4.1 22.4 1.0
CA2 A:GSH303 4.2 17.6 0.4
O A:HOH470 4.3 16.6 1.0
C36 A:5AU302 4.3 29.7 0.6
C34 A:5AU302 4.3 40.1 0.6
C14 A:5AU302 4.4 18.3 0.6
C08 A:5AU302 4.5 28.6 0.6
H A:GLY205 4.5 20.4 1.0
HN3 A:GSH303 4.6 23.8 0.4
O A:HOH561 4.6 15.6 1.0
HA3 A:GLY205 4.6 27.6 1.0
HH A:TYR7 4.7 14.8 1.0
C35 A:5AU302 4.9 33.1 0.6
HD2 A:PHE8 4.9 16.6 1.0
CD2 A:TYR108 4.9 16.2 1.0
CD1 A:TYR108 4.9 19.4 1.0
C2 A:GSH303 4.9 18.1 0.4

Arsenic binding site 2 out of 2 in 5ddl

Go back to Arsenic Binding Sites List in 5ddl
Arsenic binding site 2 out of 2 in the Crystal Structure of Wt Human Glutathione Transferase Pi Soaked with A Metalloid Then Back-Soaked with 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 Wt Human Glutathione Transferase Pi Soaked with A Metalloid Then Back-Soaked with Glutathione within 5.0Å range:
probe atom residue distance (Å) B Occ
B:As303

b:46.3
occ:0.60
AS1 B:5AU303 0.0 46.3 0.6
C32 B:5AU303 2.0 23.8 0.6
HB22 B:GSH304 2.3 24.5 0.4
S10 B:5AU303 2.4 34.2 0.6
S12 B:5AU303 2.4 42.0 0.6
C33 B:5AU303 3.0 32.6 0.6
C37 B:5AU303 3.0 25.5 0.6
OH B:TYR108 3.1 16.2 1.0
CB2 B:GSH304 3.2 20.4 0.4
HH B:TYR108 3.2 19.5 1.0
HSG B:GSH304 3.3 21.7 0.4
C09 B:5AU303 3.5 22.4 0.6
C13 B:5AU303 3.5 17.3 0.6
CZ B:TYR108 3.5 20.2 1.0
HB23 B:GSH304 3.6 24.5 0.4
SG2 B:GSH304 3.8 18.1 0.4
CE2 B:TYR108 4.1 15.6 1.0
CE1 B:TYR108 4.1 20.3 1.0
HA2 B:GSH304 4.1 21.9 0.4
HE2 B:TYR108 4.2 18.7 1.0
HE1 B:TYR108 4.2 24.4 1.0
CA2 B:GSH304 4.3 18.2 0.4
C36 B:5AU303 4.3 26.8 0.6
C34 B:5AU303 4.3 25.3 0.6
O B:HOH431 4.3 13.8 1.0
C08 B:5AU303 4.4 21.8 0.6
C14 B:5AU303 4.4 18.8 0.6
H B:GLY205 4.5 22.2 1.0
HN3 B:GSH304 4.6 29.3 0.4
HA3 B:GLY205 4.6 30.0 1.0
O B:HOH567 4.6 18.8 1.0
HG21 B:VAL10 4.7 27.1 1.0
C35 B:5AU303 4.8 29.6 0.6
HD2 B:PHE8 4.9 21.7 1.0
C2 B:GSH304 4.9 17.2 0.4
N3 B:GSH304 5.0 24.4 0.4
CD2 B:TYR108 5.0 17.1 1.0

Reference:

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.
Page generated: Mon Jul 7 00:13:54 2025

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