Fluorine in PDB 4yzn: Humanized ROCO4 Bound to Compound 19

All present enzymatic activity of Humanized ROCO4 Bound to Compound 19:
2.7.11.1;

The structure of Humanized ROCO4 Bound to Compound 19, PDB code: 4yzn was solved by B.K.Gilsbach, A.C.Messias, G.Ito, M.Sattler, D.R.Alessi, A.Wittinghofer, A.Kortholt, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	37.64 / 1.55
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	42.400, 42.400, 326.900, 90.00, 90.00, 90.00
R / Rfree (%)	18.7 / 21.6

The binding sites of Fluorine atom in the Humanized ROCO4 Bound to Compound 19 (pdb code 4yzn). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 4 binding sites of Fluorine where determined in the Humanized ROCO4 Bound to Compound 19, PDB code: 4yzn:
Jump to Fluorine binding site number: 1; 2; 3; 4;

Fluorine binding site 1 out of 4 in the Humanized ROCO4 Bound to Compound 19


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Humanized ROCO4 Bound to Compound 19 within 5.0Å range: probe atom residue distance (Å) B Occ A:F1301 b:24.4 occ:1.00 FAE A:4K51301 0.0 24.4 1.0 CBF A:4K51301 1.3 25.8 1.0 FAD A:4K51301 2.1 23.2 1.0 FAF A:4K51301 2.1 24.3 1.0 C5 A:4K51301 2.3 19.6 1.0 C6 A:4K51301 2.7 17.6 1.0 SD A:MET1105 3.3 34.0 1.0 O A:GLU1106 3.6 27.9 1.0 C4 A:4K51301 3.7 19.7 1.0 CG1 A:VAL1091 3.8 20.4 1.0 CB A:MET1105 3.9 30.6 1.0 CB A:ALA1053 3.9 26.2 1.0 N1 A:4K51301 4.1 20.9 1.0 O A:HOH1501 4.2 30.2 1.0 NAS A:4K51301 4.2 21.9 1.0 CG A:MET1105 4.4 29.7 1.0 CD1 A:LEU1161 4.6 16.1 1.0 CG2 A:VAL1091 4.7 21.3 1.0 N3 A:4K51301 4.7 19.3 1.0 C A:GLU1106 4.7 25.6 1.0 CB A:VAL1091 4.8 20.0 1.0 CE A:MET1105 4.8 34.1 1.0 CD A:LYS1055 4.9 28.2 1.0 C2 A:4K51301 4.9 19.7 1.0

Fluorine binding site 2 out of 4 in the Humanized ROCO4 Bound to Compound 19


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Humanized ROCO4 Bound to Compound 19 within 5.0Å range: probe atom residue distance (Å) B Occ A:F1301 b:24.3 occ:1.00 FAF A:4K51301 0.0 24.3 1.0 CBF A:4K51301 1.4 25.8 1.0 FAD A:4K51301 2.1 23.2 1.0 FAE A:4K51301 2.1 24.4 1.0 C5 A:4K51301 2.3 19.6 1.0 NAS A:4K51301 3.0 21.9 1.0 C4 A:4K51301 3.0 19.7 1.0 C6 A:4K51301 3.4 17.6 1.0 CG1 A:VAL1040 3.6 26.7 1.0 O A:HOH1405 3.7 30.2 1.0 CG A:LYS1055 3.7 27.3 1.0 CD A:LYS1055 3.8 28.2 1.0 SD A:MET1105 4.1 34.0 1.0 CB A:ALA1053 4.1 26.2 1.0 N3 A:4K51301 4.2 19.3 1.0 CE A:LYS1055 4.3 33.1 1.0 CBD A:4K51301 4.4 21.2 1.0 CG2 A:VAL1040 4.4 27.9 1.0 N1 A:4K51301 4.6 20.9 1.0 CB A:VAL1040 4.6 26.5 1.0 NZ A:LYS1055 4.7 35.9 1.0 O A:HOH1501 4.7 30.2 1.0 OD1 A:ASP1177 4.8 20.7 0.5 C2 A:4K51301 4.9 19.7 1.0

Fluorine binding site 3 out of 4 in the Humanized ROCO4 Bound to Compound 19


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Humanized ROCO4 Bound to Compound 19 within 5.0Å range: probe atom residue distance (Å) B Occ A:F1301 b:23.2 occ:1.00 FAD A:4K51301 0.0 23.2 1.0 CBF A:4K51301 1.3 25.8 1.0 FAF A:4K51301 2.1 24.3 1.0 FAE A:4K51301 2.1 24.4 1.0 C5 A:4K51301 2.3 19.6 1.0 NAS A:4K51301 3.0 21.9 1.0 C4 A:4K51301 3.0 19.7 1.0 O A:HOH1405 3.1 30.2 1.0 C6 A:4K51301 3.4 17.6 1.0 CD1 A:LEU1161 3.6 16.1 1.0 O A:HOH1501 3.6 30.2 1.0 OD1 A:ASP1177 3.6 20.7 0.5 CB A:ALA1176 3.9 15.8 1.0 N3 A:4K51301 4.3 19.3 1.0 CBD A:4K51301 4.4 21.2 1.0 SD A:MET1105 4.4 34.0 1.0 CG A:ASP1177 4.6 19.4 0.5 N1 A:4K51301 4.6 20.9 1.0 OD2 A:ASP1177 4.8 22.1 0.5 CD A:LYS1055 4.8 28.2 1.0 NZ A:LYS1055 4.8 35.9 1.0 CG A:LEU1161 4.8 17.9 1.0 CG1 A:VAL1091 4.8 20.4 1.0 CG2 A:VAL1091 4.9 21.3 1.0 C2 A:4K51301 5.0 19.7 1.0

Fluorine binding site 4 out of 4 in the Humanized ROCO4 Bound to Compound 19


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Humanized ROCO4 Bound to Compound 19 within 5.0Å range: probe atom residue distance (Å) B Occ A:F1301 b:30.5 occ:1.00 FAC A:4K51301 0.0 30.5 1.0 CAW A:4K51301 1.3 29.7 1.0 CAH A:4K51301 2.3 27.4 1.0 CBA A:4K51301 2.4 34.8 1.0 CAV A:4K51301 2.9 41.2 1.0 O A:HOH1509 3.2 25.9 1.0 NBE A:4K51301 3.5 50.4 1.0 OAB A:4K51301 3.5 40.1 1.0 O A:HOH1499 3.6 29.5 1.0 CAI A:4K51301 3.6 28.1 1.0 CAY A:4K51301 3.6 26.0 1.0 CAO A:4K51301 3.7 49.3 1.0 O A:ILE1032 4.0 35.2 1.0 OD1 A:ASP1112 4.0 21.6 1.0 CA A:GLY1111 4.0 19.2 1.0 CAZ A:4K51301 4.1 28.4 1.0 CAL A:4K51301 4.2 19.7 1.0 N A:ASP1112 4.4 21.3 1.0 CAK A:4K51301 4.6 56.1 1.0 CAN A:4K51301 4.7 56.9 1.0 C A:GLY1111 4.7 19.6 1.0 CBD A:4K51301 4.7 21.2 1.0 NAR A:4K51301 4.8 22.0 1.0 N3 A:4K51301 4.9 19.3 1.0 C A:ILE1032 5.0 32.5 1.0 CG A:ASP1112 5.0 22.0 1.0 CB A:ILE1032 5.0 30.1 1.0

B.K.Gilsbach, A.C.Messias, G.Ito, M.Sattler, D.R.Alessi, A.Wittinghofer, A.Kortholt. Structural Characterization of LRRK2 Inhibitors. J.Med.Chem. V. 58 3751 2015.
ISSN: ISSN 0022-2623
PubMed: 25897865
DOI: 10.1021/JM5018779