Atomistry » Thallium » PDB 1f1h-4wfh » 1fpj
Atomistry »
  Thallium »
    PDB 1f1h-4wfh »
      1fpj »

Thallium in PDB 1fpj: Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Amp, 2,5-Anhydro-D-Glucitol-1,6- Bisphosphate, Thallium (10 Mm) and Lithium Ions (10 Mm)

Enzymatic activity of Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Amp, 2,5-Anhydro-D-Glucitol-1,6- Bisphosphate, Thallium (10 Mm) and Lithium Ions (10 Mm)

All present enzymatic activity of Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Amp, 2,5-Anhydro-D-Glucitol-1,6- Bisphosphate, Thallium (10 Mm) and Lithium Ions (10 Mm):
3.1.3.11;

Protein crystallography data

The structure of Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Amp, 2,5-Anhydro-D-Glucitol-1,6- Bisphosphate, Thallium (10 Mm) and Lithium Ions (10 Mm), PDB code: 1fpj was solved by V.Villeret, W.N.Lipscomb, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 2.20
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 61.200, 166.800, 80.300, 90.00, 90.00, 90.00
R / Rfree (%) 18.9 / n/a

Thallium Binding Sites:

The binding sites of Thallium atom in the Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Amp, 2,5-Anhydro-D-Glucitol-1,6- Bisphosphate, Thallium (10 Mm) and Lithium Ions (10 Mm) (pdb code 1fpj). This binding sites where shown within 5.0 Angstroms radius around Thallium atom.
In total 4 binding sites of Thallium where determined in the Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Amp, 2,5-Anhydro-D-Glucitol-1,6- Bisphosphate, Thallium (10 Mm) and Lithium Ions (10 Mm), PDB code: 1fpj:
Jump to Thallium binding site number: 1; 2; 3; 4;

Thallium binding site 1 out of 4 in 1fpj

Go back to Thallium Binding Sites List in 1fpj
Thallium binding site 1 out of 4 in the Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Amp, 2,5-Anhydro-D-Glucitol-1,6- Bisphosphate, Thallium (10 Mm) and Lithium Ions (10 Mm)


Mono view


Stereo pair view

A full contact list of Thallium with other atoms in the Tl binding site number 1 of Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Amp, 2,5-Anhydro-D-Glucitol-1,6- Bisphosphate, Thallium (10 Mm) and Lithium Ions (10 Mm) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Tl336

b:35.6
occ:0.63
 OD1 A:ASP118 2.8 19.6 1.0
O A:LEU120 2.9 17.7 1.0
OE2 A:GLU97 2.9 51.2 1.0
OE2 A:GLU98 3.1 43.8 1.0
CD A:GLU97 3.3 44.1 1.0
OE1 A:GLU97 3.3 46.7 1.0
OG A:SER123 3.6 40.7 1.0
CG A:ASP118 3.8 20.5 1.0
C A:LEU120 3.8 17.9 1.0
O3P A:AHG339 3.9 47.2 1.0
OD2 A:ASP118 4.0 22.4 1.0
CA A:ASP121 4.3 19.4 1.0
CD A:GLU98 4.3 37.4 1.0
N A:ASP121 4.4 18.7 1.0
CG A:GLU97 4.5 38.4 1.0
N A:LEU120 4.6 17.7 1.0
CB A:GLU97 4.6 29.2 1.0
CB A:SER123 4.6 33.8 1.0
CA A:LEU120 4.7 19.9 1.0

Thallium binding site 2 out of 4 in 1fpj

Go back to Thallium Binding Sites List in 1fpj
Thallium binding site 2 out of 4 in the Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Amp, 2,5-Anhydro-D-Glucitol-1,6- Bisphosphate, Thallium (10 Mm) and Lithium Ions (10 Mm)


Mono view


Stereo pair view

A full contact list of Thallium with other atoms in the Tl binding site number 2 of Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Amp, 2,5-Anhydro-D-Glucitol-1,6- Bisphosphate, Thallium (10 Mm) and Lithium Ions (10 Mm) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Tl337

b:47.1
occ:0.50
 OE2 A:GLU280 2.8 27.6 1.0
OE1 A:GLU280 3.0 25.2 1.0
NH1 A:ARG276 3.2 50.1 1.0
CD A:GLU280 3.3 23.9 1.0
O1 A:AHG339 3.9 40.2 1.0
OE2 A:GLU97 4.1 51.2 1.0
CD2 A:LEU275 4.1 14.0 1.0
O A:LYS274 4.1 21.4 1.0
C2 A:AHG339 4.3 27.8 1.0
CZ A:ARG276 4.3 51.6 1.0
C1 A:AHG339 4.4 31.4 1.0
CD A:ARG276 4.5 32.6 1.0
CA A:LEU275 4.6 17.5 1.0
OD1 A:ASP121 4.6 22.9 1.0
CG A:LYS274 4.7 22.6 1.0
CG A:GLU280 4.8 20.5 1.0
N A:ARG276 4.8 16.7 1.0
CE A:LYS274 4.8 25.4 1.0
C A:LYS274 4.8 20.7 1.0
NE A:ARG276 4.8 44.9 1.0
CD A:GLU97 4.9 44.1 1.0
NH1 A:ARG313 5.0 32.8 1.0

Thallium binding site 3 out of 4 in 1fpj

Go back to Thallium Binding Sites List in 1fpj
Thallium binding site 3 out of 4 in the Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Amp, 2,5-Anhydro-D-Glucitol-1,6- Bisphosphate, Thallium (10 Mm) and Lithium Ions (10 Mm)


Mono view


Stereo pair view

A full contact list of Thallium with other atoms in the Tl binding site number 3 of Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Amp, 2,5-Anhydro-D-Glucitol-1,6- Bisphosphate, Thallium (10 Mm) and Lithium Ions (10 Mm) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Tl336

b:38.8
occ:0.55
 OD1 B:ASP118 2.8 23.9 1.0
O B:LEU120 2.9 17.9 1.0
OE2 B:GLU97 3.2 51.3 1.0
OE2 B:GLU98 3.3 55.1 1.0
OE1 B:GLU97 3.4 47.9 1.0
CD B:GLU97 3.5 44.7 1.0
C B:LEU120 3.7 16.7 1.0
CG B:ASP118 3.8 20.9 1.0
O1P B:AHG339 3.8 38.0 1.0
OD2 B:ASP118 4.0 25.7 1.0
OG B:SER123 4.1 37.3 1.0
CA B:ASP121 4.2 16.8 1.0
N B:ASP121 4.3 15.2 1.0
N B:LEU120 4.5 18.2 1.0
CD B:GLU98 4.5 50.3 1.0
CB B:SER123 4.6 30.7 1.0
CB B:GLU97 4.7 30.7 1.0
CA B:LEU120 4.7 17.4 1.0
CG B:GLU97 4.7 40.1 1.0

Thallium binding site 4 out of 4 in 1fpj

Go back to Thallium Binding Sites List in 1fpj
Thallium binding site 4 out of 4 in the Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Amp, 2,5-Anhydro-D-Glucitol-1,6- Bisphosphate, Thallium (10 Mm) and Lithium Ions (10 Mm)


Mono view


Stereo pair view

A full contact list of Thallium with other atoms in the Tl binding site number 4 of Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Amp, 2,5-Anhydro-D-Glucitol-1,6- Bisphosphate, Thallium (10 Mm) and Lithium Ions (10 Mm) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Tl337

b:50.3
occ:0.45
 OE2 B:GLU280 2.8 25.2 1.0
OE1 B:GLU280 3.0 22.6 1.0
CD B:GLU280 3.3 20.4 1.0
NH1 B:ARG276 3.4 41.1 1.0
OE2 B:GLU97 3.7 51.3 1.0
O B:LYS274 4.1 19.5 1.0
O1 B:AHG339 4.2 36.7 1.0
CD2 B:LEU275 4.3 13.7 1.0
CD B:GLU97 4.4 44.7 1.0
CD B:ARG276 4.5 30.6 1.0
C2 B:AHG339 4.6 20.3 1.0
CA B:LEU275 4.6 19.3 1.0
CZ B:ARG276 4.6 43.8 1.0
C1 B:AHG339 4.6 27.4 1.0
CE B:LYS274 4.7 20.0 1.0
N B:ARG276 4.7 21.3 1.0
OD1 B:ASP121 4.7 22.8 1.0
CG B:GLU280 4.8 17.4 1.0
CG B:LYS274 4.8 20.6 1.0
C B:LYS274 4.9 20.1 1.0
NH1 B:ARG313 4.9 39.4 1.0
O1P B:AHG339 4.9 38.0 1.0
O3P B:AHG339 5.0 45.8 1.0

Reference:

V.Villeret, S.Huang, H.J.Fromm, W.N.Lipscomb. Crystallographic Evidence For the Action of Potassium, Thallium, and Lithium Ions on Fructose-1,6-Bisphosphatase. Proc.Natl.Acad.Sci.Usa V. 92 8916 1995.
ISSN: ISSN 0027-8424
PubMed: 7568043
DOI: 10.1073/PNAS.92.19.8916
Page generated: Tue Aug 19 06:21:54 2025

Last articles

Zn in 9UUO
Zn in 9UUS
Zn in 9W4R
Zn in 9VKW
Zn in 9W4S
Zn in 9VH1
Zn in 9RMX
Zn in 9RMU
Zn in 9QWN
Zn in 9U9Y
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy