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Fluorine in PDB 2fjm: The Structure of Phosphotyrosine Phosphatase 1B in Complex with Compound 2

Enzymatic activity of The Structure of Phosphotyrosine Phosphatase 1B in Complex with Compound 2

All present enzymatic activity of The Structure of Phosphotyrosine Phosphatase 1B in Complex with Compound 2:
3.1.3.48;

Protein crystallography data

The structure of The Structure of Phosphotyrosine Phosphatase 1B in Complex with Compound 2, PDB code: 2fjm was solved by E.Asante-Appiah, S.Patel, C.Desponts, J.M.Taylor, C.Lau, C.Dufresne, M.Therien, R.Friesen, J.W.Becker, Y.Leblanc, G.Scapin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.00 / 2.10
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 86.431, 86.621, 139.193, 90.00, 90.00, 90.00
R / Rfree (%) 19.2 / 21.7

Other elements in 2fjm:

The structure of The Structure of Phosphotyrosine Phosphatase 1B in Complex with Compound 2 also contains other interesting chemical elements:

Magnesium (Mg) 1 atom
Chlorine (Cl) 2 atoms

Fluorine Binding Sites:

The binding sites of Fluorine atom in the The Structure of Phosphotyrosine Phosphatase 1B in Complex with Compound 2 (pdb code 2fjm). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 4 binding sites of Fluorine where determined in the The Structure of Phosphotyrosine Phosphatase 1B in Complex with Compound 2, PDB code: 2fjm:
Jump to Fluorine binding site number: 1; 2; 3; 4;

Fluorine binding site 1 out of 4 in 2fjm

Go back to Fluorine Binding Sites List in 2fjm
Fluorine binding site 1 out of 4 in the The Structure of Phosphotyrosine Phosphatase 1B in Complex with Compound 2


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of The Structure of Phosphotyrosine Phosphatase 1B in Complex with Compound 2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F800

b:28.0
occ:1.00
 F30 A:073800 0.0 28.0 1.0
C28 A:073800 1.3 28.8 1.0
F29 A:073800 2.1 28.8 1.0
C5 A:073800 2.3 27.9 1.0
P31 A:073800 2.6 28.8 1.0
C4 A:073800 2.7 28.6 1.0
O A:HOH802 2.8 28.7 1.0
O32 A:073800 2.8 27.2 1.0
O33 A:073800 3.1 28.2 1.0
CE1 A:PHE682 3.5 43.0 1.0
C6 A:073800 3.5 29.3 1.0
CG A:GLN762 3.6 39.3 1.0
CZ A:PHE682 3.6 42.4 1.0
CB A:GLN762 3.8 40.0 1.0
CA A:GLY720 3.8 41.2 1.0
CD1 A:PHE682 3.8 41.5 1.0
O34 A:073800 3.9 27.6 1.0
N A:GLY720 4.0 41.4 1.0
CE2 A:PHE682 4.0 42.4 1.0
C3 A:073800 4.0 26.5 1.0
CG A:PHE682 4.3 41.8 1.0
CD2 A:PHE682 4.3 42.8 1.0
N A:PHE682 4.4 42.1 1.0
C1 A:073800 4.6 29.9 1.0
CD A:GLN762 4.7 40.8 1.0
CG1 A:ILE719 4.7 41.0 1.0
OE1 A:GLN762 4.8 43.2 1.0
C2 A:073800 4.9 29.2 1.0
N A:ARG721 4.9 41.4 1.0
C A:GLY720 4.9 41.2 1.0
CA A:PHE682 4.9 41.7 1.0

Fluorine binding site 2 out of 4 in 2fjm

Go back to Fluorine Binding Sites List in 2fjm
Fluorine binding site 2 out of 4 in the The Structure of Phosphotyrosine Phosphatase 1B in Complex with Compound 2


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of The Structure of Phosphotyrosine Phosphatase 1B in Complex with Compound 2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F800

b:28.8
occ:1.00
 F29 A:073800 0.0 28.8 1.0
C28 A:073800 1.3 28.8 1.0
F30 A:073800 2.1 28.0 1.0
C5 A:073800 2.3 27.9 1.0
P31 A:073800 2.6 28.8 1.0
C6 A:073800 2.7 29.3 1.0
O32 A:073800 2.9 27.2 1.0
O34 A:073800 3.1 27.6 1.0
O A:HOH802 3.2 28.7 1.0
CE2 A:PHE682 3.5 42.4 1.0
CB A:ASP681 3.5 43.9 1.0
C4 A:073800 3.6 28.6 1.0
CD2 A:PHE682 3.7 42.8 1.0
NH2 A:ARG721 3.7 40.4 1.0
N A:PHE682 3.7 42.1 1.0
O33 A:073800 3.8 28.2 1.0
CZ A:PHE682 3.8 42.4 1.0
CA A:ASP681 3.9 43.2 1.0
C1 A:073800 4.1 29.9 1.0
CG A:PHE682 4.2 41.8 1.0
C A:ASP681 4.2 42.5 1.0
CE1 A:PHE682 4.3 43.0 1.0
NE A:ARG721 4.3 40.5 1.0
CZ A:ARG721 4.4 41.1 1.0
CD1 A:PHE682 4.4 41.5 1.0
CG A:ASP681 4.7 46.8 1.0
C3 A:073800 4.7 26.5 1.0
CA A:PHE682 4.7 41.7 1.0
OD2 A:ASP681 4.8 48.5 1.0
C2 A:073800 4.9 29.2 1.0

Fluorine binding site 3 out of 4 in 2fjm

Go back to Fluorine Binding Sites List in 2fjm
Fluorine binding site 3 out of 4 in the The Structure of Phosphotyrosine Phosphatase 1B in Complex with Compound 2


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of The Structure of Phosphotyrosine Phosphatase 1B in Complex with Compound 2 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F801

b:28.6
occ:1.00
 F30 B:073801 0.0 28.6 1.0
C28 B:073801 1.3 28.9 1.0
F29 B:073801 2.2 29.7 1.0
C5 B:073801 2.2 27.0 1.0
P31 B:073801 2.6 28.9 1.0
C4 B:073801 2.6 27.9 1.0
O B:HOH804 2.8 27.9 1.0
O32 B:073801 2.9 26.5 1.0
O33 B:073801 3.1 28.4 1.0
C6 B:073801 3.5 28.5 1.0
CE1 B:PHE682 3.5 43.0 1.0
CG B:GLN762 3.5 38.5 1.0
CZ B:PHE682 3.6 42.5 1.0
CB B:GLN762 3.8 39.3 1.0
CD1 B:PHE682 3.8 41.0 1.0
CA B:GLY720 3.8 40.5 1.0
O34 B:073801 3.9 27.8 1.0
C3 B:073801 4.0 26.8 1.0
CE2 B:PHE682 4.0 42.6 1.0
N B:GLY720 4.1 40.7 1.0
CG B:PHE682 4.3 40.8 1.0
CD2 B:PHE682 4.3 42.1 1.0
N B:PHE682 4.5 41.3 1.0
C1 B:073801 4.6 28.8 1.0
CD B:GLN762 4.7 41.7 1.0
CG1 B:ILE719 4.7 41.3 1.0
C2 B:073801 4.8 29.0 1.0
OE1 B:GLN762 4.8 41.9 1.0
N B:ARG721 4.9 40.7 1.0
C B:GLY720 4.9 40.2 1.0
CA B:PHE682 4.9 41.2 1.0

Fluorine binding site 4 out of 4 in 2fjm

Go back to Fluorine Binding Sites List in 2fjm
Fluorine binding site 4 out of 4 in the The Structure of Phosphotyrosine Phosphatase 1B in Complex with Compound 2


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of The Structure of Phosphotyrosine Phosphatase 1B in Complex with Compound 2 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F801

b:29.7
occ:1.00
 F29 B:073801 0.0 29.7 1.0
C28 B:073801 1.3 28.9 1.0
F30 B:073801 2.2 28.6 1.0
C5 B:073801 2.3 27.0 1.0
P31 B:073801 2.6 28.9 1.0
C6 B:073801 2.7 28.5 1.0
O32 B:073801 3.0 26.5 1.0
O34 B:073801 3.0 27.8 1.0
O B:HOH804 3.3 27.9 1.0
CB B:ASP681 3.5 43.3 1.0
CE2 B:PHE682 3.5 42.6 1.0
C4 B:073801 3.6 27.9 1.0
NH2 B:ARG721 3.6 38.9 1.0
CD2 B:PHE682 3.7 42.1 1.0
O33 B:073801 3.8 28.4 1.0
N B:PHE682 3.8 41.3 1.0
CZ B:PHE682 3.9 42.5 1.0
CA B:ASP681 3.9 42.5 1.0
C1 B:073801 4.1 28.8 1.0
CG B:PHE682 4.2 40.8 1.0
C B:ASP681 4.3 41.9 1.0
CE1 B:PHE682 4.3 43.0 1.0
NE B:ARG721 4.3 41.2 1.0
CZ B:ARG721 4.3 39.4 1.0
CD1 B:PHE682 4.5 41.0 1.0
C3 B:073801 4.7 26.8 1.0
CG B:ASP681 4.7 45.9 1.0
OD2 B:ASP681 4.7 48.9 1.0
CA B:PHE682 4.8 41.2 1.0
C2 B:073801 4.9 29.0 1.0

Reference:

E.Asante-Appiah, S.Patel, C.Desponts, J.M.Taylor, C.Lau, C.Dufresne, M.Therien, R.Friesen, J.W.Becker, Y.Leblanc, B.P.Kennedy, G.Scapin. Conformation-Assisted Inhibition of Protein-Tyrosine Phosphatase-1B Elicits Inhibitor Selectivity Over T-Cell Protein-Tyrosine Phosphatase. J.Biol.Chem. V. 281 8010 2006.
ISSN: ISSN 0021-9258
PubMed: 16407290
DOI: 10.1074/JBC.M511827200
Page generated: Wed Jul 31 14:10:31 2024

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