Atomistry » Arsenic » PDB 4zt2-5hr7 » 5dal
Atomistry »
  Arsenic »
    PDB 4zt2-5hr7 »
      5dal »

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

Enzymatic activity of Crystal Structure of Human Glutathione Transferase Pi Complexed with A Metalloid in the Presence of Glutathione

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

Protein crystallography data

The structure of Crystal Structure of Human Glutathione Transferase Pi Complexed with A Metalloid in the Presence of Glutathione, PDB code: 5dal 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) 34.00 / 1.50
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 77.550, 90.220, 68.670, 90.00, 98.01, 90.00
R / Rfree (%) 18 / 21.3

Arsenic Binding Sites:

The binding sites of Arsenic atom in the Crystal Structure of Human Glutathione Transferase Pi Complexed with A Metalloid in the Presence of Glutathione (pdb code 5dal). This binding sites where shown within 5.0 Angstroms radius around Arsenic atom.
In total 4 binding sites of Arsenic where determined in the Crystal Structure of Human Glutathione Transferase Pi Complexed with A Metalloid in the Presence of Glutathione, PDB code: 5dal:
Jump to Arsenic binding site number: 1; 2; 3; 4;

Arsenic binding site 1 out of 4 in 5dal

Go back to Arsenic Binding Sites List in 5dal
Arsenic binding site 1 out of 4 in the Crystal Structure of Human Glutathione Transferase Pi Complexed with A Metalloid in the Presence 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 Presence of Glutathione within 5.0Å range:
probe atom residue distance (Å) B Occ
A:As302

b:32.1
occ:0.60
 AS1 A:5AU302 0.0 32.1 0.6
HSG A:GSH303 1.8 30.7 0.4
C32 A:5AU302 2.1 26.3 0.6
S10 A:5AU302 2.3 33.4 0.6
S12 A:5AU302 2.4 28.9 0.6
HB23 A:GSH303 2.5 27.3 0.4
SG2 A:GSH303 2.7 25.6 0.4
H13A A:5AU302 3.0 24.9 0.6
C37 A:5AU302 3.0 29.9 0.6
CB2 A:GSH303 3.0 22.8 0.4
C33 A:5AU302 3.1 26.9 0.6
H37 A:5AU302 3.1 35.9 0.6
H09A A:5AU302 3.2 33.7 0.6
H33 A:5AU302 3.2 32.3 0.6
HH A:TYR108 3.2 29.8 1.0
OH A:TYR108 3.3 24.8 1.0
C13 A:5AU302 3.4 20.8 0.6
C09 A:5AU302 3.4 28.1 0.6
HB22 A:GSH303 3.5 27.3 0.4
CZ A:TYR108 3.6 22.9 1.0
O A:HOH415 3.6 32.2 1.0
HE2 A:TYR108 3.9 27.7 1.0
CE2 A:TYR108 3.9 23.1 1.0
H08 A:5AU302 3.9 29.4 0.6
H13 A:5AU302 4.0 24.9 0.6
O A:HOH470 4.1 21.0 1.0
H09 A:5AU302 4.2 33.7 0.6
CA2 A:GSH303 4.2 21.1 0.4
HA2 A:GSH303 4.3 25.3 0.4
O A:HOH584 4.3 23.8 1.0
CE1 A:TYR108 4.3 24.6 1.0
C36 A:5AU302 4.3 26.9 0.6
C34 A:5AU302 4.4 26.4 0.6
C08 A:5AU302 4.4 24.5 0.6
HH A:TYR7 4.5 21.6 1.0
C14 A:5AU302 4.5 23.8 0.6
HE1 A:TYR108 4.5 29.6 1.0
H A:GLY205 4.6 27.6 1.0
HN27 A:5AU302 4.6 25.9 0.6
OH A:TYR7 4.8 18.0 1.0
CD2 A:TYR108 4.8 21.7 1.0
HA3 A:GLY205 4.9 30.0 1.0
C35 A:5AU302 4.9 32.3 0.6

Arsenic binding site 2 out of 4 in 5dal

Go back to Arsenic Binding Sites List in 5dal
Arsenic binding site 2 out of 4 in the Crystal Structure of Human Glutathione Transferase Pi Complexed with A Metalloid in the Presence 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 Presence of Glutathione within 5.0Å range:
probe atom residue distance (Å) B Occ
A:As304

b:26.9
occ:0.60
 AS7 A:PA0304 0.0 26.9 0.6
C1 A:PA0304 2.0 34.1 0.6
SG A:CYS101 2.6 29.6 1.0
C2 A:PA0304 2.9 36.8 0.6
H2 A:PA0304 2.9 44.2 0.6
O43 A:5AU302 3.0 26.5 0.6
HB2 A:CYS101 3.0 24.6 1.0
HG A:CYS101 3.1 35.6 1.0
C6 A:PA0304 3.1 27.7 0.6
H6 A:PA0304 3.2 33.2 0.6
HA A:CYS101 3.3 23.5 1.0
CB A:CYS101 3.3 20.5 1.0
HH21 A:ARG13 3.4 25.5 1.0
O A:HOH564 3.5 36.2 1.0
H41 A:5AU302 3.6 25.7 0.6
C42 A:5AU302 3.7 21.8 0.6
CA A:CYS101 3.8 19.6 1.0
HH22 A:ARG13 3.8 25.5 1.0
NH2 A:ARG13 4.0 21.3 1.0
H41A A:5AU302 4.0 25.7 0.6
C41 A:5AU302 4.0 21.4 0.6
HG B:CYS101 4.1 31.1 1.0
HB3 A:CYS101 4.2 24.6 1.0
C3 A:PA0304 4.2 39.2 0.6
O A:HOH460 4.3 31.6 1.0
C5 A:PA0304 4.4 33.5 0.6
OE2 A:GLU97 4.4 13.9 0.5
HD12 A:ILE104 4.5 23.7 1.0
O44 A:5AU302 4.6 19.7 0.6
C A:CYS101 4.7 18.8 1.0
HB A:ILE104 4.7 25.3 1.0
O A:CYS101 4.7 20.5 1.0
C4 A:PA0304 4.8 34.6 0.6
HD13 A:ILE104 4.9 23.7 1.0
N A:CYS101 4.9 16.1 1.0
HG23 A:ILE104 5.0 26.5 1.0

Arsenic binding site 3 out of 4 in 5dal

Go back to Arsenic Binding Sites List in 5dal
Arsenic binding site 3 out of 4 in the Crystal Structure of Human Glutathione Transferase Pi Complexed with A Metalloid in the Presence of Glutathione


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 3 of Crystal Structure of Human Glutathione Transferase Pi Complexed with A Metalloid in the Presence of Glutathione within 5.0Å range:
probe atom residue distance (Å) B Occ
B:As303

b:30.1
occ:0.58
 AS1 B:5AU303 0.0 30.1 0.6
C32 B:5AU303 2.0 30.0 0.6
HSG B:GSH304 2.3 31.8 0.4
S10 B:5AU303 2.3 31.3 0.6
S12 B:5AU303 2.4 27.7 0.6
HB22 B:GSH304 2.5 25.3 0.4
SG2 B:GSH304 2.8 26.5 0.4
C37 B:5AU303 3.0 31.7 0.6
C33 B:5AU303 3.0 30.4 0.6
H09A B:5AU303 3.0 28.2 0.6
H37 B:5AU303 3.1 38.0 0.6
CB2 B:GSH304 3.1 21.1 0.4
H13A B:5AU303 3.1 24.2 0.6
H33 B:5AU303 3.2 36.4 0.6
HH B:TYR108 3.2 27.0 1.0
OH B:TYR108 3.2 22.5 1.0
C09 B:5AU303 3.3 23.5 0.6
C13 B:5AU303 3.4 20.2 0.6
O B:HOH420 3.5 31.0 1.0
HB23 B:GSH304 3.6 25.3 0.4
CZ B:TYR108 3.6 24.1 1.0
O B:HOH418 3.7 21.1 1.0
HE2 B:TYR108 3.9 26.5 1.0
CE2 B:TYR108 3.9 22.1 1.0
H09 B:5AU303 3.9 28.2 0.6
H14 B:5AU303 4.0 24.3 0.6
O B:HOH597 4.0 20.9 1.0
H08 B:5AU303 4.1 27.3 0.6
H13 B:5AU303 4.2 24.2 0.6
HH B:TYR7 4.3 21.5 1.0
HA2 B:GSH304 4.3 24.4 0.4
CE1 B:TYR108 4.3 25.2 1.0
CA2 B:GSH304 4.3 20.3 0.4
C36 B:5AU303 4.3 39.6 0.6
C34 B:5AU303 4.3 27.6 0.6
C08 B:5AU303 4.4 22.8 0.6
C14 B:5AU303 4.4 20.3 0.6
HE1 B:TYR108 4.5 30.2 1.0
H B:GLY205 4.6 25.3 1.0
OH B:TYR7 4.7 17.9 1.0
CD2 B:TYR108 4.8 21.2 1.0
C35 B:5AU303 4.9 27.7 0.6
HN3 B:GSH304 5.0 28.3 0.4

Arsenic binding site 4 out of 4 in 5dal

Go back to Arsenic Binding Sites List in 5dal
Arsenic binding site 4 out of 4 in the Crystal Structure of Human Glutathione Transferase Pi Complexed with A Metalloid in the Presence of Glutathione


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 4 of Crystal Structure of Human Glutathione Transferase Pi Complexed with A Metalloid in the Presence of Glutathione within 5.0Å range:
probe atom residue distance (Å) B Occ
B:As305

b:24.4
occ:0.60
 AS7 B:PA0305 0.0 24.4 0.6
C1 B:PA0305 2.0 29.8 0.6
SG B:CYS101 2.7 25.9 1.0
C2 B:PA0305 2.8 28.4 0.6
H2 B:PA0305 2.9 34.1 0.6
O43 B:5AU303 3.0 27.7 0.6
C6 B:PA0305 3.0 23.6 0.6
HB2 B:CYS101 3.1 21.8 1.0
HA B:CYS101 3.1 20.2 1.0
HG B:CYS101 3.2 31.1 1.0
H6 B:PA0305 3.2 28.3 0.6
CB B:CYS101 3.3 18.1 1.0
HH21 B:ARG13 3.4 24.9 1.0
H41 B:5AU303 3.5 28.1 0.6
C42 B:5AU303 3.7 18.2 0.6
CA B:CYS101 3.7 16.9 1.0
HH22 B:ARG13 3.8 24.9 1.0
NH2 B:ARG13 3.9 20.7 1.0
C41 B:5AU303 4.0 23.4 0.6
H41A B:5AU303 4.2 28.1 0.6
C3 B:PA0305 4.2 34.6 0.6
HG A:CYS101 4.2 35.6 1.0
HB3 B:CYS101 4.2 21.8 1.0
C5 B:PA0305 4.3 26.0 0.6
O B:HOH421 4.5 28.6 1.0
O44 B:5AU303 4.5 22.0 0.6
O B:CYS101 4.5 18.3 1.0
C B:CYS101 4.6 16.2 1.0
HD11 B:ILE104 4.6 25.4 1.0
OE2 B:GLU97 4.6 26.2 1.0
HB B:ILE104 4.6 19.6 1.0
C4 B:PA0305 4.8 31.4 0.6
N B:CYS101 4.9 13.1 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: Wed Jul 10 12:46:42 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy