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Thallium in PDB 1fpk: Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Thallium Ions (10 Mm)

Enzymatic activity of Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Thallium Ions (10 Mm)

All present enzymatic activity of Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Thallium 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 Thallium Ions (10 Mm), PDB code: 1fpk 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 / 3.00
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 132.600, 132.600, 67.700, 90.00, 90.00, 120.00
R / Rfree (%) 22.6 / 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 Thallium Ions (10 Mm) (pdb code 1fpk). This binding sites where shown within 5.0 Angstroms radius around Thallium atom.
In total 6 binding sites of Thallium where determined in the Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Thallium Ions (10 Mm), PDB code: 1fpk:
Jump to Thallium binding site number: 1; 2; 3; 4; 5; 6;

Thallium binding site 1 out of 6 in 1fpk

Go back to Thallium Binding Sites List in 1fpk
Thallium binding site 1 out of 6 in the Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Thallium 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 Thallium Ions (10 Mm) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Tl336

b:40.0
occ:0.45
 OE2 A:GLU97 2.4 48.8 1.0
OE1 A:GLU280 2.6 37.2 1.0
OD2 A:ASP118 2.6 40.9 1.0
OD1 A:ASP121 2.9 13.2 1.0
CD A:GLU280 3.0 25.9 1.0
OE2 A:GLU280 3.5 26.4 1.0
CG A:ASP118 3.5 35.5 1.0
CD A:GLU97 3.5 45.5 1.0
TL A:TL338 3.6 40.0 0.7
NH1 A:ARG276 3.7 47.0 1.0
TL A:TL337 3.9 40.0 0.7
CG A:GLU280 3.9 18.9 1.0
OE1 A:GLU97 4.1 46.8 1.0
CG A:ASP121 4.1 30.7 1.0
OD1 A:ASP118 4.2 39.2 1.0
CB A:ASP118 4.4 23.9 1.0
CZ A:ARG276 4.5 49.1 1.0
CB A:ASP121 4.6 21.3 1.0
CG A:GLU97 4.7 39.1 1.0
CA A:ASP121 4.8 23.5 1.0

Thallium binding site 2 out of 6 in 1fpk

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Thallium binding site 2 out of 6 in the Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Thallium 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 Thallium Ions (10 Mm) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Tl337

b:40.0
occ:0.70
 O A:LEU120 2.1 32.1 1.0
OD1 A:ASP118 2.7 39.2 1.0
OE1 A:GLU97 2.8 46.8 1.0
C A:LEU120 3.0 20.1 1.0
CA A:ASP121 3.4 23.5 1.0
CG A:ASP118 3.4 35.5 1.0
OD2 A:ASP118 3.4 40.9 1.0
N A:ASP121 3.5 20.7 1.0
CD A:GLU97 3.6 45.5 1.0
OE2 A:GLU97 3.7 48.8 1.0
TL A:TL336 3.9 40.0 0.5
N A:GLY122 4.1 30.5 1.0
CA A:LEU120 4.2 16.4 1.0
N A:LEU120 4.2 16.3 1.0
OE2 A:GLU98 4.3 55.2 1.0
C A:ASP121 4.3 28.6 1.0
OD2 A:ASP74 4.3 33.9 1.0
OG A:SER123 4.3 40.6 1.0
CB A:ASP121 4.4 21.3 1.0
OD1 A:ASP121 4.7 13.2 1.0
CB A:ASP118 4.8 23.9 1.0
CB A:LEU120 4.9 12.8 1.0
CG A:ASP121 5.0 30.7 1.0

Thallium binding site 3 out of 6 in 1fpk

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Thallium binding site 3 out of 6 in the Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Thallium 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 Thallium Ions (10 Mm) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Tl338

b:40.0
occ:0.67
 OE1 A:GLU280 2.9 37.2 1.0
TL A:TL336 3.6 40.0 0.5
NH1 A:ARG276 3.8 47.0 1.0
CD A:GLU280 3.8 25.9 1.0
OE2 A:GLU280 4.0 26.4 1.0
CD2 A:LEU275 4.2 5.5 1.0
OD1 A:ASP121 4.2 13.2 1.0
CG A:LEU275 4.2 7.3 1.0
CA A:LEU275 4.5 17.3 1.0
CB A:LEU275 4.6 12.5 1.0
CE A:LYS274 4.7 34.0 1.0
CD A:LYS274 4.7 26.5 1.0
NZ A:LYS274 4.8 38.6 1.0
CG A:LYS274 4.8 27.8 1.0
N A:LEU275 5.0 22.7 1.0

Thallium binding site 4 out of 6 in 1fpk

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Thallium binding site 4 out of 6 in the Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Thallium 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 Thallium Ions (10 Mm) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Tl336

b:40.0
occ:0.49
 OE1 B:GLU97 2.5 53.7 1.0
OE1 B:GLU280 2.6 55.9 1.0
OD2 B:ASP118 2.6 49.4 1.0
CD B:GLU280 3.1 50.7 1.0
CG B:ASP118 3.4 44.6 1.0
CD B:GLU97 3.4 52.0 1.0
OD1 B:ASP121 3.4 39.9 1.0
OE2 B:GLU280 3.5 51.6 1.0
TL B:TL338 3.6 40.0 0.7
OE2 B:GLU97 3.7 55.5 1.0
OD1 B:ASP118 3.8 49.5 1.0
TL B:TL337 3.9 40.0 0.7
CG B:GLU280 4.0 45.3 1.0
CB B:ASP118 4.4 35.7 1.0
CG B:ASP121 4.5 41.4 1.0
CB B:ASP121 4.7 35.7 1.0
CG B:GLU97 4.7 45.2 1.0
CA B:ASP121 4.8 33.2 1.0
CB B:GLU97 4.9 35.5 1.0
NE B:ARG276 4.9 52.3 1.0

Thallium binding site 5 out of 6 in 1fpk

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Thallium binding site 5 out of 6 in the Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Thallium Ions (10 Mm)


Mono view


Stereo pair view

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

b:40.0
occ:0.65
 O B:LEU120 2.2 45.9 1.0
OE2 B:GLU97 2.6 55.5 1.0
OD1 B:ASP118 2.7 49.5 1.0
OE2 B:GLU98 3.1 51.6 1.0
C B:LEU120 3.2 30.8 1.0
CA B:ASP121 3.4 33.2 1.0
CD B:GLU97 3.5 52.0 1.0
CG B:ASP118 3.6 44.6 1.0
OD2 B:ASP118 3.6 49.4 1.0
N B:ASP121 3.6 25.3 1.0
OG B:SER123 3.8 57.0 1.0
TL B:TL336 3.9 40.0 0.5
OE1 B:GLU97 4.0 53.7 1.0
N B:GLY122 4.1 38.5 1.0
CD B:GLU98 4.1 53.5 1.0
C B:ASP121 4.2 37.6 1.0
CA B:LEU120 4.3 26.0 1.0
OE1 B:GLU98 4.3 53.8 1.0
N B:LEU120 4.4 26.3 1.0
CG B:GLU97 4.5 45.2 1.0
CB B:ASP121 4.5 35.7 1.0
OD1 B:ASP121 4.9 39.9 1.0
N B:SER123 4.9 54.5 1.0
OD2 B:ASP74 4.9 37.2 1.0
CB B:ASP118 5.0 35.7 1.0

Thallium binding site 6 out of 6 in 1fpk

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Thallium binding site 6 out of 6 in the Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Thallium Ions (10 Mm)


Mono view


Stereo pair view

A full contact list of Thallium with other atoms in the Tl binding site number 6 of Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Thallium Ions (10 Mm) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Tl338

b:40.0
occ:0.68
 OE1 B:GLU280 2.9 55.9 1.0
TL B:TL336 3.6 40.0 0.5
CD B:GLU280 3.8 50.7 1.0
OE2 B:GLU280 3.8 51.6 1.0
OD1 B:ASP121 4.2 39.9 1.0
CE B:LYS274 4.5 28.6 1.0
CG B:LEU275 4.6 29.6 1.0
CD2 B:LEU275 4.6 24.5 1.0
CA B:LEU275 4.7 30.6 1.0
CG B:LYS274 4.8 21.3 1.0
CD B:LYS274 4.8 24.2 1.0
CB B:LEU275 4.8 27.5 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: Fri Oct 11 09:15:57 2024

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