Fluorine in PDB 2g72: Structure of Hpnmt with Inhibitor 3-Fluoromethyl-7- Thiomorpholinosulfonamide-Thiq and Adomet

All present enzymatic activity of Structure of Hpnmt with Inhibitor 3-Fluoromethyl-7- Thiomorpholinosulfonamide-Thiq and Adomet:
2.1.1.28;

The structure of Structure of Hpnmt with Inhibitor 3-Fluoromethyl-7- Thiomorpholinosulfonamide-Thiq and Adomet, PDB code: 2g72 was solved by J.D.A.Tyndall, C.L.Gee, J.L.Martin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	31.01 / 2.00
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	94.310, 94.310, 188.890, 90.00, 90.00, 90.00
R / Rfree (%)	22.6 / 26.2

The binding sites of Fluorine atom in the Structure of Hpnmt with Inhibitor 3-Fluoromethyl-7- Thiomorpholinosulfonamide-Thiq and Adomet (pdb code 2g72). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Structure of Hpnmt with Inhibitor 3-Fluoromethyl-7- Thiomorpholinosulfonamide-Thiq and Adomet, PDB code: 2g72:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Structure of Hpnmt with Inhibitor 3-Fluoromethyl-7- Thiomorpholinosulfonamide-Thiq and Adomet


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Structure of Hpnmt with Inhibitor 3-Fluoromethyl-7- Thiomorpholinosulfonamide-Thiq and Adomet within 5.0Å range: probe atom residue distance (Å) B Occ A:F4001 b:62.6 occ:1.00 F1 A:F214001 0.0 62.6 1.0 C11 A:F214001 1.4 40.7 1.0 C3 A:F214001 2.4 42.8 1.0 OE2 A:GLU219 2.9 43.3 1.0 N2 A:F214001 3.1 40.6 1.0 CD2 A:TYR222 3.4 38.3 1.0 CE2 A:TYR222 3.5 35.2 1.0 C4 A:F214001 3.6 37.6 1.0 CB A:ALA186 3.7 43.4 1.0 CD A:GLU219 3.7 45.4 1.0 OE1 A:GLU219 3.8 41.1 1.0 CE A:SAM2001 3.9 57.0 1.0 CG A:TYR222 4.0 37.9 1.0 CG2 A:VAL231 4.1 45.9 1.0 CZ A:TYR222 4.2 38.1 1.0 C1 A:F214001 4.4 39.7 1.0 O A:PHE182 4.6 42.3 1.0 CD1 A:TYR222 4.6 42.5 1.0 CB A:TYR222 4.6 40.9 1.0 CA A:ALA186 4.7 46.8 1.0 CE1 A:TYR222 4.7 39.1 1.0 CB A:PHE182 4.7 35.2 1.0 CB A:ALA216 4.8 38.4 1.0 CG1 A:VAL231 4.8 42.3 1.0 C10 A:F214001 4.8 36.9 1.0 OH A:TYR222 4.9 42.5 1.0 CD2 A:PHE182 4.9 29.5 1.0

Fluorine binding site 2 out of 2 in the Structure of Hpnmt with Inhibitor 3-Fluoromethyl-7- Thiomorpholinosulfonamide-Thiq and Adomet


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Structure of Hpnmt with Inhibitor 3-Fluoromethyl-7- Thiomorpholinosulfonamide-Thiq and Adomet within 5.0Å range: probe atom residue distance (Å) B Occ B:F4002 b:58.3 occ:1.00 F1 B:F214002 0.0 58.3 1.0 C11 B:F214002 1.4 44.4 1.0 C3 B:F214002 2.4 43.5 1.0 C4 B:F214002 3.0 42.2 1.0 O B:HOH4010 3.1 46.4 1.0 CE B:SAM2002 3.2 53.4 1.0 CE2 B:TYR222 3.6 42.6 1.0 N2 B:F214002 3.6 40.3 1.0 CD2 B:TYR222 3.7 39.1 1.0 CB B:ALA186 3.7 36.6 1.0 CZ B:TYR222 3.8 41.6 1.0 OE2 B:GLU219 3.8 44.8 1.0 CG B:TYR222 3.9 40.8 1.0 CE1 B:TYR222 4.0 40.3 1.0 CD1 B:TYR222 4.1 43.6 1.0 O B:PHE182 4.2 35.5 1.0 CB B:PHE182 4.3 34.5 1.0 OH B:TYR222 4.3 48.1 1.0 C10 B:F214002 4.5 41.7 1.0 OH B:TYR35 4.7 45.9 1.0 CE1 B:TYR35 4.7 41.6 1.0 CB B:TYR222 4.8 42.8 1.0 C1 B:F214002 4.8 41.7 1.0 SD B:SAM2002 4.8 58.9 1.0 CD B:GLU219 4.8 46.4 1.0 CG2 B:VAL231 4.8 54.8 1.0 CA B:ALA186 5.0 40.1 1.0 CG B:PHE182 5.0 36.2 1.0

C.L.Gee, N.Drinkwater, J.D.A.Tyndall, G.L.Grunewald, Q.Wu, M.J.Mcleish, J.L.Martin. Enzyme Adaptation to Inhibitor Binding: A Cryptic Binding Site in Phenylethanolamine N-Methyltransferase J.Med.Chem. V. 50 4845 2007.
ISSN: ISSN 0022-2623
PubMed: 17845018
DOI: 10.1021/JM0703385