Fluorine in PDB 1kav: Human Tyrosine Phosphatase 1B Complexed with An Inhibitor

All present enzymatic activity of Human Tyrosine Phosphatase 1B Complexed with An Inhibitor:
3.1.3.48;

The structure of Human Tyrosine Phosphatase 1B Complexed with An Inhibitor, PDB code: 1kav was solved by Z.Jia, Q.Ye, A.N.Dinaut, Q.Wang, D.Waddleton, P.Payette, C.Ramachandran, B.Kennedy, G.Hum, S.D.Taylor, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	6.00 / 2.35
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	89.220, 89.220, 108.782, 90.00, 90.00, 120.00
R / Rfree (%)	20 / 25

The binding sites of Fluorine atom in the Human Tyrosine Phosphatase 1B Complexed with An Inhibitor (pdb code 1kav). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 4 binding sites of Fluorine where determined in the Human Tyrosine Phosphatase 1B Complexed with An Inhibitor, PDB code: 1kav:
Jump to Fluorine binding site number: 1; 2; 3; 4;

Fluorine binding site 1 out of 4 in the Human Tyrosine Phosphatase 1B Complexed with An Inhibitor


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Human Tyrosine Phosphatase 1B Complexed with An Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:F301 b:21.9 occ:1.00 F1 A:FEP301 0.0 21.9 1.0 C5 A:FEP301 1.5 23.8 1.0 F2 A:FEP301 2.2 27.3 1.0 C9 A:FEP301 2.2 23.7 1.0 C8 A:FEP301 2.5 24.6 1.0 P1 A:FEP301 2.6 21.6 1.0 O A:HOH408 2.7 22.9 1.0 OP3 A:FEP301 3.0 21.4 1.0 OP2 A:FEP301 3.1 16.7 1.0 CE1 A:PHE182 3.2 9.0 1.0 CG A:GLN262 3.3 18.1 1.0 CD1 A:PHE182 3.5 12.8 1.0 C10 A:FEP301 3.6 22.2 1.0 CB A:GLN262 3.7 17.0 1.0 CA A:GLY220 3.8 15.9 1.0 CZ A:PHE182 3.8 11.9 1.0 C7 A:FEP301 3.9 27.3 1.0 OP1 A:FEP301 4.0 18.7 1.0 N A:GLY220 4.0 18.2 1.0 OE1 A:GLN262 4.1 24.2 1.0 CD A:GLN262 4.2 22.1 1.0 CG A:PHE182 4.4 15.8 1.0 N A:PHE182 4.5 20.6 1.0 CE2 A:PHE182 4.6 15.0 1.0 C11 A:FEP301 4.7 26.5 1.0 CG1 A:ILE219 4.7 17.7 1.0 C6 A:FEP301 4.8 30.0 1.0 N A:ARG221 4.8 17.5 1.0 CD2 A:PHE182 4.8 13.0 1.0 C A:GLY220 4.8 17.7 1.0 CA A:PHE182 4.9 19.6 1.0

Fluorine binding site 2 out of 4 in the Human Tyrosine Phosphatase 1B Complexed with An Inhibitor


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Human Tyrosine Phosphatase 1B Complexed with An Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:F301 b:27.3 occ:1.00 F2 A:FEP301 0.0 27.3 1.0 C5 A:FEP301 1.1 23.8 1.0 C9 A:FEP301 1.9 23.7 1.0 F1 A:FEP301 2.2 21.9 1.0 C10 A:FEP301 2.5 22.2 1.0 P1 A:FEP301 2.5 21.6 1.0 OP2 A:FEP301 3.1 16.7 1.0 O A:HOH408 3.1 22.9 1.0 OP1 A:FEP301 3.1 18.7 1.0 C8 A:FEP301 3.2 24.6 1.0 NH2 A:ARG221 3.6 16.6 1.0 CZ A:PHE182 3.6 11.9 1.0 CE1 A:PHE182 3.7 9.0 1.0 N A:PHE182 3.8 20.6 1.0 OP3 A:FEP301 3.8 21.4 1.0 CE2 A:PHE182 3.8 15.0 1.0 C11 A:FEP301 3.8 26.5 1.0 CD1 A:PHE182 4.0 12.8 1.0 CB A:ASP181 4.0 30.9 1.0 CD2 A:PHE182 4.1 13.0 1.0 CA A:ASP181 4.1 26.4 1.0 CG A:PHE182 4.1 15.8 1.0 CZ A:ARG221 4.3 17.7 1.0 C7 A:FEP301 4.3 27.3 1.0 OD1 A:ASP181 4.3 39.1 1.0 NE A:ARG221 4.4 16.3 1.0 C A:ASP181 4.4 23.8 1.0 C6 A:FEP301 4.6 30.0 1.0 CA A:PHE182 4.7 19.6 1.0 CG A:ASP181 4.7 37.1 1.0

Fluorine binding site 3 out of 4 in the Human Tyrosine Phosphatase 1B Complexed with An Inhibitor


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Human Tyrosine Phosphatase 1B Complexed with An Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:F301 b:76.7 occ:1.00 F3 A:FEP301 0.0 76.7 1.0 C12 A:FEP301 1.5 75.0 1.0 F4 A:FEP301 2.2 77.7 1.0 C16 A:FEP301 2.2 72.5 1.0 P2 A:FEP301 2.6 77.0 1.0 C17 A:FEP301 2.9 68.6 1.0 O A:HOH502 3.0 40.2 1.0 OP5 A:FEP301 3.0 75.7 1.0 NH2 A:ARG47 3.1 61.5 1.0 C15 A:FEP301 3.1 69.5 1.0 OP6 A:FEP301 3.1 75.6 1.0 CZ A:ARG47 3.9 60.4 1.0 OP4 A:FEP301 4.1 75.8 1.0 C18 A:FEP301 4.1 64.7 1.0 C14 A:FEP301 4.2 65.2 1.0 NH1 A:ARG47 4.4 62.2 1.0 C13 A:FEP301 4.6 62.8 1.0 NE A:ARG47 4.7 58.1 1.0

Fluorine binding site 4 out of 4 in the Human Tyrosine Phosphatase 1B Complexed with An Inhibitor


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Human Tyrosine Phosphatase 1B Complexed with An Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:F301 b:77.7 occ:1.00 F4 A:FEP301 0.0 77.7 1.0 C12 A:FEP301 1.1 75.0 1.0 C16 A:FEP301 1.9 72.5 1.0 F3 A:FEP301 2.2 76.7 1.0 C17 A:FEP301 2.4 68.6 1.0 P2 A:FEP301 2.5 77.0 1.0 O A:HOH502 3.1 40.2 1.0 OP5 A:FEP301 3.1 75.7 1.0 OP4 A:FEP301 3.2 75.8 1.0 C15 A:FEP301 3.2 69.5 1.0 C18 A:FEP301 3.8 64.7 1.0 NH2 A:ARG47 3.8 61.5 1.0 OP6 A:FEP301 3.8 75.6 1.0 CZ A:ARG47 4.0 60.4 1.0 C14 A:FEP301 4.3 65.2 1.0 NE A:ARG47 4.4 58.1 1.0 NH1 A:ARG47 4.5 62.2 1.0 C13 A:FEP301 4.6 62.8 1.0

Z.Jia, Q.Ye, A.N.Dinaut, Q.Wang, D.Waddleton, P.Payette, C.Ramachandran, B.Kennedy, G.Hum, S.D.Taylor. Structure of Protein Tyrosine Phosphatase 1B in Complex with Inhibitors Bearing Two Phosphotyrosine Mimetics. J.Med.Chem. V. 44 4584 2001.
ISSN: ISSN 0022-2623
PubMed: 11741477
DOI: 10.1021/JM010266W