Fluorine in PDB 1bzc: Human PTP1B Catalytic Domain Complexed with Tpi

All present enzymatic activity of Human PTP1B Catalytic Domain Complexed with Tpi:
3.1.3.48;

The structure of Human PTP1B Catalytic Domain Complexed with Tpi, PDB code: 1bzc was solved by M.R.Groves, Z.J.Yao, T.R.Jr Burke, D.Barford, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	14.00 / 2.35
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	88.470, 88.470, 104.620, 90.00, 90.00, 120.00
R / Rfree (%)	20.4 / 25.6

The binding sites of Fluorine atom in the Human PTP1B Catalytic Domain Complexed with Tpi (pdb code 1bzc). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Human PTP1B Catalytic Domain Complexed with Tpi, PDB code: 1bzc:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Human PTP1B Catalytic Domain Complexed with Tpi


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Human PTP1B Catalytic Domain Complexed with Tpi within 5.0Å range: probe atom residue distance (Å) B Occ A:F902 b:15.3 occ:1.00 F1 A:TPI902 0.0 15.3 1.0 C1 A:TPI902 1.4 12.8 1.0 F2 A:TPI902 2.2 15.7 1.0 C3 A:TPI902 2.3 11.4 1.0 P A:TPI902 2.6 15.7 1.0 C4 A:TPI902 2.7 9.6 1.0 O A:HOH914 2.8 10.0 1.0 O2 A:TPI902 3.0 17.9 1.0 O3 A:TPI902 3.1 19.4 1.0 CB A:ASP181 3.2 24.6 1.0 NH2 A:ARG221 3.3 8.9 1.0 N A:PHE182 3.5 18.2 1.0 CA A:ASP181 3.6 19.4 1.0 C2 A:TPI902 3.6 11.1 1.0 CZ A:PHE182 3.9 5.8 1.0 C A:ASP181 3.9 20.2 1.0 NE A:ARG221 3.9 6.4 1.0 O1 A:TPI902 3.9 19.7 1.0 CZ A:ARG221 3.9 8.0 1.0 CE2 A:PHE182 3.9 2.3 1.0 CE1 A:PHE182 4.0 7.4 1.0 CD2 A:PHE182 4.0 8.0 1.0 C5 A:TPI902 4.0 6.3 1.0 CD1 A:PHE182 4.1 7.0 1.0 CG A:PHE182 4.1 8.6 1.0 CG A:ASP181 4.5 29.7 1.0 CA A:PHE182 4.5 18.9 1.0 OD2 A:ASP181 4.7 36.3 1.0 C10 A:TPI902 4.7 10.2 1.0 C11 A:TPI902 4.9 10.2 1.0 CB A:PHE182 4.9 14.6 1.0 O A:ASP181 5.0 18.7 1.0 N A:ASP181 5.0 14.7 1.0 NH1 A:ARG221 5.0 12.1 1.0

Fluorine binding site 2 out of 2 in the Human PTP1B Catalytic Domain Complexed with Tpi


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Human PTP1B Catalytic Domain Complexed with Tpi within 5.0Å range: probe atom residue distance (Å) B Occ A:F902 b:15.7 occ:1.00 F2 A:TPI902 0.0 15.7 1.0 C1 A:TPI902 1.3 12.8 1.0 F1 A:TPI902 2.2 15.3 1.0 C3 A:TPI902 2.3 11.4 1.0 P A:TPI902 2.5 15.7 1.0 O A:HOH914 2.7 10.0 1.0 C2 A:TPI902 2.8 11.1 1.0 O2 A:TPI902 3.0 17.9 1.0 O1 A:TPI902 3.0 19.7 1.0 CE1 A:PHE182 3.3 7.4 1.0 CG A:GLN262 3.4 16.0 1.0 C4 A:TPI902 3.6 9.6 1.0 CD1 A:PHE182 3.7 7.0 1.0 CA A:GLY220 3.7 5.6 1.0 CZ A:PHE182 3.8 5.8 1.0 CB A:GLN262 3.8 14.8 1.0 N A:GLY220 3.8 8.1 1.0 O3 A:TPI902 3.9 19.4 1.0 C10 A:TPI902 4.2 10.2 1.0 CG A:PHE182 4.4 8.6 1.0 CD A:GLN262 4.4 17.5 1.0 CE2 A:PHE182 4.5 2.3 1.0 OE1 A:GLN262 4.5 19.5 1.0 CG1 A:ILE219 4.6 5.9 1.0 N A:PHE182 4.6 18.2 1.0 C5 A:TPI902 4.7 6.3 1.0 N A:ARG221 4.8 9.0 1.0 C A:GLY220 4.8 5.4 1.0 CD2 A:PHE182 4.8 8.0 1.0 C11 A:TPI902 4.9 10.2 1.0

M.R.Groves, Z.J.Yao, P.P.Roller, T.R.Burke Jr., D.Barford. Structural Basis For Inhibition of the Protein Tyrosine Phosphatase 1B By Phosphotyrosine Peptide Mimetics. Biochemistry V. 37 17773 1998.
ISSN: ISSN 0006-2960
PubMed: 9922143
DOI: 10.1021/BI9816958