Fluorine in PDB 3el8: Crystal Structure of C-Src in Complex with Pyrazolopyrimidine 5

All present enzymatic activity of Crystal Structure of C-Src in Complex with Pyrazolopyrimidine 5:
2.7.10.2;

The structure of Crystal Structure of C-Src in Complex with Pyrazolopyrimidine 5, PDB code: 3el8 was solved by A.C.Dar, M.S.Lopez, K.M.Shokat, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.30
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	42.375, 63.693, 73.792, 101.01, 90.25, 90.12
R / Rfree (%)	21.8 / 26.2

The binding sites of Fluorine atom in the Crystal Structure of C-Src in Complex with Pyrazolopyrimidine 5 (pdb code 3el8). 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 C-Src in Complex with Pyrazolopyrimidine 5, PDB code: 3el8:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Crystal Structure of C-Src in Complex with Pyrazolopyrimidine 5


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 C-Src in Complex with Pyrazolopyrimidine 5 within 5.0Å range: probe atom residue distance (Å) B Occ A:F601 b:78.4 occ:1.00 FAF A:PD5601 0.0 78.4 1.0 CBG A:PD5601 1.3 77.9 1.0 FAE A:PD5601 2.2 78.8 1.0 FAG A:PD5601 2.2 76.0 1.0 CBA A:PD5601 2.3 77.0 1.0 CAK A:PD5601 2.9 76.6 1.0 CAP A:PD5601 3.4 76.2 1.0 CD1 A:LEU317 3.6 54.0 1.0 CD1 A:LEU322 4.0 38.9 1.0 CG A:MET314 4.1 66.8 1.0 CB A:LEU317 4.2 54.1 1.0 CAH A:PD5601 4.2 76.6 1.0 CB A:LEU322 4.5 32.9 1.0 CG A:LEU317 4.5 54.5 1.0 CAY A:PD5601 4.6 75.9 1.0 CA A:MET314 4.7 67.5 1.0 O A:VAL323 4.7 31.9 1.0 CG A:LEU322 4.8 39.1 1.0 CB A:MET314 4.8 67.6 1.0 OD1 A:ASP404 4.9 69.5 1.0 CAJ A:PD5601 4.9 76.1 1.0 SD A:MET314 5.0 67.7 1.0

Fluorine binding site 2 out of 3 in the Crystal Structure of C-Src in Complex with Pyrazolopyrimidine 5


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 C-Src in Complex with Pyrazolopyrimidine 5 within 5.0Å range: probe atom residue distance (Å) B Occ A:F601 b:76.0 occ:1.00 FAG A:PD5601 0.0 76.0 1.0 CBG A:PD5601 1.3 77.9 1.0 FAE A:PD5601 2.2 78.8 1.0 FAF A:PD5601 2.2 78.4 1.0 CBA A:PD5601 2.3 77.0 1.0 CAK A:PD5601 2.9 76.6 1.0 OD1 A:ASP404 3.4 69.5 1.0 CAP A:PD5601 3.5 76.2 1.0 O A:HOH139 3.8 55.3 1.0 CAH A:PD5601 4.2 76.6 1.0 CD1 A:LEU317 4.3 54.0 1.0 ND1 A:HIS384 4.3 40.5 1.0 CE1 A:HIS384 4.4 39.9 1.0 CG1 A:VAL402 4.5 30.2 1.0 CD1 A:LEU322 4.5 38.9 1.0 CG A:ASP404 4.6 67.1 1.0 CAY A:PD5601 4.6 75.9 1.0 CA A:ALA403 4.8 45.5 1.0 CD2 A:LEU322 4.8 38.7 1.0 CAJ A:PD5601 4.9 76.1 1.0 O A:VAL402 4.9 32.9 1.0

Fluorine binding site 3 out of 3 in the Crystal Structure of C-Src in Complex with Pyrazolopyrimidine 5


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 C-Src in Complex with Pyrazolopyrimidine 5 within 5.0Å range: probe atom residue distance (Å) B Occ A:F601 b:78.8 occ:1.00 FAE A:PD5601 0.0 78.8 1.0 CBG A:PD5601 1.3 77.9 1.0 FAF A:PD5601 2.2 78.4 1.0 FAG A:PD5601 2.2 76.0 1.0 CBA A:PD5601 2.4 77.0 1.0 CAP A:PD5601 2.7 76.2 1.0 O A:VAL402 3.4 32.9 1.0 CAK A:PD5601 3.6 76.6 1.0 CA A:ALA403 3.8 45.5 1.0 C A:VAL402 4.0 34.7 1.0 OD1 A:ASP404 4.0 69.5 1.0 CAY A:PD5601 4.1 75.9 1.0 N A:ALA403 4.2 39.6 1.0 CB A:LEU322 4.2 32.9 1.0 OAD A:PD5601 4.2 74.2 1.0 O A:VAL323 4.2 31.9 1.0 N A:VAL323 4.3 32.0 1.0 C A:ALA403 4.6 50.0 1.0 CD1 A:LEU322 4.6 38.9 1.0 CA A:LEU322 4.6 32.1 1.0 CD2 A:LEU322 4.6 38.7 1.0 CG1 A:VAL402 4.7 30.2 1.0 CB A:ALA403 4.7 43.8 1.0 CG A:LEU322 4.7 39.1 1.0 C A:LEU322 4.7 31.9 1.0 CAH A:PD5601 4.8 76.6 1.0 N A:ASP404 4.9 56.8 1.0 CB A:VAL323 4.9 32.5 1.0 CAJ A:PD5601 5.0 76.1 1.0 NAU A:PD5601 5.0 75.2 1.0 CA A:VAL323 5.0 32.5 1.0

A.C.Dar, M.S.Lopez, K.M.Shokat. Small Molecule Recognition of C-Src Via the Imatinib-Binding Conformation. Chem.Biol. V. 15 1015 2008.
ISSN: ISSN 1074-5521
PubMed: 18940662
DOI: 10.1016/J.CHEMBIOL.2008.09.007