Fluorine in PDB 3fzr: Crystal Structure of PYK2 Complexed with Pf-431396

All present enzymatic activity of Crystal Structure of PYK2 Complexed with Pf-431396:
2.7.10.2;

The structure of Crystal Structure of PYK2 Complexed with Pf-431396, PDB code: 3fzr was solved by S.Han, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	17.88 / 2.70
Space group	P 4 21 2
Cell size a, b, c (Å), α, β, γ (°)	107.326, 107.326, 75.786, 90.00, 90.00, 90.00
R / Rfree (%)	21.1 / 27.4

The binding sites of Fluorine atom in the Crystal Structure of PYK2 Complexed with Pf-431396 (pdb code 3fzr). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Crystal Structure of PYK2 Complexed with Pf-431396, PDB code: 3fzr:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Crystal Structure of PYK2 Complexed with Pf-431396


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structure of PYK2 Complexed with Pf-431396 within 5.0Å range: probe atom residue distance (Å) B Occ A:F999 b:44.6 occ:1.00 F29 A:3JZ999 0.0 44.6 1.0 C8 A:3JZ999 1.5 42.8 1.0 F28 A:3JZ999 2.2 43.9 1.0 F27 A:3JZ999 2.4 44.5 1.0 C6 A:3JZ999 2.4 34.1 1.0 C5 A:3JZ999 3.0 31.2 1.0 N10 A:3JZ999 3.1 35.3 1.0 O A:HOH2 3.2 52.8 1.0 C7 A:3JZ999 3.5 33.2 1.0 CD1 A:LEU556 3.5 34.4 1.0 CG1 A:VAL487 3.7 42.0 1.0 OD2 A:ASP567 3.8 64.9 1.0 O A:HOH15 3.9 48.2 1.0 O A:GLY566 4.1 59.0 1.0 N4 A:3JZ999 4.2 26.1 1.0 CB A:VAL487 4.2 43.0 1.0 C17 A:3JZ999 4.3 38.7 1.0 CG2 A:VAL487 4.3 42.1 1.0 CE A:MET502 4.6 62.9 1.0 C12 A:3JZ999 4.6 35.6 1.0 N2 A:3JZ999 4.7 32.1 1.0 CG A:LEU556 4.7 36.9 1.0 CG A:MET502 4.7 60.1 1.0 CG A:ASP567 4.7 71.5 1.0 CD2 A:LEU556 4.8 42.3 1.0 C3 A:3JZ999 4.8 30.6 1.0 CB A:MET502 4.8 55.5 1.0 CB A:ASP567 4.9 55.2 1.0 C13 A:3JZ999 4.9 41.1 1.0

Fluorine binding site 2 out of 3 in the Crystal Structure of PYK2 Complexed with Pf-431396


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Crystal Structure of PYK2 Complexed with Pf-431396 within 5.0Å range: probe atom residue distance (Å) B Occ A:F999 b:43.9 occ:1.00 F28 A:3JZ999 0.0 43.9 1.0 C8 A:3JZ999 1.3 42.8 1.0 F29 A:3JZ999 2.2 44.6 1.0 C6 A:3JZ999 2.3 34.1 1.0 F27 A:3JZ999 2.4 44.5 1.0 C5 A:3JZ999 2.8 31.2 1.0 N10 A:3JZ999 2.8 35.3 1.0 C7 A:3JZ999 3.4 33.2 1.0 CG A:MET502 3.5 60.1 1.0 O A:HOH2 3.6 52.8 1.0 CB A:MET502 3.6 55.5 1.0 CB A:ALA455 3.8 41.7 1.0 N4 A:3JZ999 4.0 26.1 1.0 C12 A:3JZ999 4.2 35.6 1.0 OD2 A:ASP567 4.3 64.9 1.0 N2 A:3JZ999 4.5 32.1 1.0 CE A:MET502 4.5 62.9 1.0 C3 A:3JZ999 4.6 30.6 1.0 CG1 A:VAL439 4.8 36.6 1.0 SD A:MET502 4.8 65.7 1.0 O A:GLU503 4.8 49.8 1.0

Fluorine binding site 3 out of 3 in the Crystal Structure of PYK2 Complexed with Pf-431396


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Crystal Structure of PYK2 Complexed with Pf-431396 within 5.0Å range: probe atom residue distance (Å) B Occ A:F999 b:44.5 occ:1.00 F27 A:3JZ999 0.0 44.5 1.0 C8 A:3JZ999 1.4 42.8 1.0 C6 A:3JZ999 2.3 34.1 1.0 F29 A:3JZ999 2.4 44.6 1.0 C7 A:3JZ999 2.4 33.2 1.0 F28 A:3JZ999 2.4 43.9 1.0 CB A:MET502 3.1 55.5 1.0 O A:GLU503 3.2 49.8 1.0 C5 A:3JZ999 3.6 31.2 1.0 CG1 A:VAL487 3.6 42.0 1.0 CG A:MET502 3.7 60.1 1.0 CB A:VAL487 3.7 43.0 1.0 N2 A:3JZ999 3.8 32.1 1.0 CE1 A:TYR505 4.1 24.3 1.0 CG2 A:VAL487 4.3 42.1 1.0 N10 A:3JZ999 4.4 35.3 1.0 CE A:MET502 4.4 62.9 1.0 CD1 A:TYR505 4.4 27.0 1.0 C A:GLU503 4.4 50.6 1.0 CA A:MET502 4.4 52.1 1.0 C3 A:3JZ999 4.5 30.6 1.0 N A:GLU503 4.5 52.4 1.0 N4 A:3JZ999 4.5 26.1 1.0 C A:MET502 4.6 57.2 1.0 SD A:MET502 4.6 65.7 1.0 CB A:ALA455 4.7 41.7 1.0 CD1 A:LEU556 4.8 34.4 1.0 CA A:VAL487 5.0 41.1 1.0

S.Han, A.Mistry, J.S.Chang, D.Cunningham, M.Griffor, P.C.Bonnette, H.Wang, B.A.Chrunyk, G.E.Aspnes, D.P.Walker, A.D.Brosius, L.Buckbinder. Structural Characterization of Proline-Rich Tyrosine Kinase 2 (PYK2) Reveals A Unique (Dfg-Out) Conformation and Enables Inhibitor Design. J.Biol.Chem. V. 284 13193 2009.
ISSN: ISSN 0021-9258
PubMed: 19244237
DOI: 10.1074/JBC.M809038200