Chlorine in PDB 8udv: The X-Ray Co-Crystal Structure of Human FGFR3 V555M and Compound 17

All present enzymatic activity of The X-Ray Co-Crystal Structure of Human FGFR3 V555M and Compound 17:
2.7.10.1;

The structure of The X-Ray Co-Crystal Structure of Human FGFR3 V555M and Compound 17, PDB code: 8udv was solved by J.S.Tyhonas, L.D.Arnold, J.Cox, A.Franovic, E.Gardiner, K.Grandinetti, R.Kania, T.Kanouni, M.Lardy, C.Li, E.S.Martin, N.Miller, A.Mohan, E.A.Murphy, M.Perez, L.Soroceanu, N.Timple, S.Uryu, S.Womble, S.W.Kaldor, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.74 / 2.35
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	170.664, 54.513, 128.718, 90, 120.22, 90
R / Rfree (%)	23.6 / 26.1

The binding sites of Chlorine atom in the The X-Ray Co-Crystal Structure of Human FGFR3 V555M and Compound 17 (pdb code 8udv). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the The X-Ray Co-Crystal Structure of Human FGFR3 V555M and Compound 17, PDB code: 8udv:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the The X-Ray Co-Crystal Structure of Human FGFR3 V555M and Compound 17


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of The X-Ray Co-Crystal Structure of Human FGFR3 V555M and Compound 17 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1003 b:54.6 occ:1.00 CL1 A:WIQ1003 0.0 54.6 1.0 C15 A:WIQ1003 1.7 54.5 1.0 HG22 A:VAL486 2.6 38.4 0.0 HG21 A:VAL486 2.6 38.2 0.0 C14 A:WIQ1003 2.7 54.4 1.0 HG13 A:VAL486 2.7 38.7 0.0 C6 A:WIQ1003 2.7 54.3 1.0 HB2 A:LYS508 2.7 37.2 0.0 HG11 A:VAL486 2.8 38.5 0.0 CG2 A:VAL486 3.0 40.0 1.0 C5 A:WIQ1003 3.0 54.1 1.0 CG1 A:VAL486 3.1 40.1 1.0 HG3 A:MET555 3.3 31.8 0.0 HB1 A:ALA506 3.6 30.9 0.0 CB A:VAL486 3.7 39.6 1.0 HD2 A:LYS508 3.7 44.5 0.0 C4 A:WIQ1003 3.8 54.1 1.0 CB A:LYS508 3.8 39.1 1.0 HG23 A:VAL486 4.0 38.5 0.0 C13 A:WIQ1003 4.0 54.4 1.0 HB2 A:MET555 4.0 29.1 0.0 C7 A:WIQ1003 4.0 54.3 1.0 HG12 A:VAL486 4.1 39.0 0.0 HB3 A:ALA506 4.1 30.8 0.0 HA A:LYS508 4.2 36.4 0.0 N A:LYS508 4.2 36.4 1.0 CG A:MET555 4.2 34.1 1.0 HB2 A:PHE483 4.2 47.9 0.0 CA A:LYS508 4.3 37.7 1.0 CB A:ALA506 4.4 32.3 1.0 HA A:VAL486 4.4 38.1 0.0 HB3 A:LYS508 4.4 37.3 0.0 H A:LYS508 4.4 34.9 0.0 HB A:VAL486 4.4 38.5 0.0 HG2 A:MET555 4.4 32.1 0.0 C A:VAL507 4.5 36.0 1.0 C8 A:WIQ1003 4.5 54.4 1.0 HB3 A:PHE483 4.5 47.6 0.0 CG A:LYS508 4.6 42.6 1.0 CD A:LYS508 4.6 46.6 1.0 CB A:MET555 4.6 31.0 1.0 HG3 A:LYS508 4.6 41.1 0.0 HE2 A:MET555 4.7 36.8 0.0 CA A:VAL486 4.7 39.0 1.0 O A:VAL507 4.7 36.2 1.0 C A:ALA506 4.8 33.3 1.0 N1 A:WIQ1003 4.8 53.4 1.0 HB3 A:MET555 4.9 28.8 0.0 CB A:PHE483 4.9 50.1 1.0 O A:PHE483 4.9 49.0 1.0 N A:VAL507 4.9 33.7 1.0 O A:ALA506 4.9 33.6 1.0 C3 A:WIQ1003 4.9 54.1 1.0 HD3 A:LYS508 5.0 44.5 0.0

Chlorine binding site 2 out of 3 in the The X-Ray Co-Crystal Structure of Human FGFR3 V555M and Compound 17


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of The X-Ray Co-Crystal Structure of Human FGFR3 V555M and Compound 17 within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl803 b:62.2 occ:1.00 CL1 B:WIQ803 0.0 62.2 1.0 C15 B:WIQ803 1.7 61.7 1.0 HG22 B:VAL486 2.6 33.0 0.0 HG21 B:VAL486 2.6 32.9 0.0 HG13 B:VAL486 2.7 33.1 0.0 C14 B:WIQ803 2.7 61.7 1.0 C6 B:WIQ803 2.7 61.1 1.0 HB2 B:LYS508 2.7 23.1 0.0 HG11 B:VAL486 2.8 33.0 0.0 C5 B:WIQ803 3.0 60.0 1.0 CG2 B:VAL486 3.0 36.4 1.0 HE3 B:MET555 3.0 41.4 0.0 CG1 B:VAL486 3.1 36.6 1.0 HE1 B:MET555 3.2 41.5 0.0 CE B:MET555 3.5 45.3 1.0 HB1 B:ALA506 3.6 19.7 0.0 CB B:VAL486 3.7 36.1 1.0 HD2 B:LYS508 3.7 31.6 0.0 C4 B:WIQ803 3.7 59.0 1.0 CB B:LYS508 3.8 26.6 1.0 C13 B:WIQ803 4.0 61.7 1.0 HG23 B:VAL486 4.0 33.3 0.0 C7 B:WIQ803 4.0 61.4 1.0 SD B:MET555 4.0 44.6 1.0 HG12 B:VAL486 4.1 33.4 0.0 HA B:LYS508 4.1 21.9 0.0 HB3 B:ALA506 4.2 19.5 0.0 N B:LYS508 4.2 24.3 1.0 HB2 B:MET555 4.2 21.3 0.0 CA B:LYS508 4.3 24.9 1.0 HB3 B:PHE483 4.3 46.9 0.0 HB2 B:PHE483 4.3 47.1 0.0 HB3 B:LYS508 4.4 23.3 0.0 HA B:VAL486 4.4 32.7 0.0 CB B:ALA506 4.4 23.4 1.0 H B:LYS508 4.4 20.9 0.0 C B:VAL507 4.4 24.1 1.0 HB B:VAL486 4.4 33.1 0.0 C8 B:WIQ803 4.5 61.6 1.0 HE2 B:MET555 4.5 41.6 0.0 CG B:LYS508 4.6 30.4 1.0 O B:VAL507 4.6 24.1 1.0 CD B:LYS508 4.6 34.9 1.0 HG3 B:LYS508 4.6 27.5 0.0 CA B:VAL486 4.7 35.6 1.0 N1 B:WIQ803 4.8 56.1 1.0 C B:ALA506 4.8 23.9 1.0 CB B:PHE483 4.8 50.7 1.0 C3 B:WIQ803 4.8 58.0 1.0 O B:PHE483 4.9 50.0 1.0 N B:VAL507 4.9 23.7 1.0 O B:ALA506 4.9 24.2 1.0 HD3 B:LYS508 4.9 31.8 0.0

Chlorine binding site 3 out of 3 in the The X-Ray Co-Crystal Structure of Human FGFR3 V555M and Compound 17


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of The X-Ray Co-Crystal Structure of Human FGFR3 V555M and Compound 17 within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl1004 b:53.2 occ:1.00 CL1 C:WIQ1004 0.0 53.2 1.0 C15 C:WIQ1004 1.7 53.5 1.0 HG12 C:VAL486 2.3 40.1 0.0 HG11 C:VAL486 2.5 40.1 0.0 C14 C:WIQ1004 2.7 53.5 1.0 HB2 C:LYS508 2.7 31.7 0.0 C6 C:WIQ1004 2.7 53.6 1.0 CG1 C:VAL486 2.8 42.8 1.0 C5 C:WIQ1004 3.0 53.6 1.0 HG3 C:MET555 3.2 27.9 0.0 HB C:VAL486 3.4 39.7 0.0 HB1 C:ALA506 3.6 27.1 0.0 HG13 C:VAL486 3.7 40.5 0.0 CB C:VAL486 3.7 42.3 1.0 HD2 C:LYS508 3.7 40.7 0.0 CB C:LYS508 3.8 34.6 1.0 C4 C:WIQ1004 3.8 53.9 1.0 C13 C:WIQ1004 3.9 53.5 1.0 HB2 C:MET555 4.0 25.2 0.0 C7 C:WIQ1004 4.0 53.6 1.0 HA C:LYS508 4.1 30.2 0.0 HB3 C:ALA506 4.1 27.0 0.0 CG C:MET555 4.2 31.3 1.0 N C:LYS508 4.2 31.8 1.0 CA C:LYS508 4.3 32.7 1.0 HB2 C:PHE483 4.3 48.6 0.0 HA C:VAL486 4.3 39.0 0.0 HB3 C:LYS508 4.4 31.8 0.0 HB3 C:PHE483 4.4 48.5 0.0 H C:LYS508 4.4 28.9 0.0 CB C:ALA506 4.4 30.1 1.0 HG2 C:MET555 4.4 28.1 0.0 C C:VAL507 4.5 31.4 1.0 C8 C:WIQ1004 4.5 53.5 1.0 HD13 C:ILE539 4.5 30.3 0.0 CG C:LYS508 4.6 39.0 1.0 HG21 C:VAL486 4.6 40.6 0.0 CB C:MET555 4.6 28.5 1.0 CD C:LYS508 4.6 43.5 1.0 HG3 C:LYS508 4.6 36.7 0.0 HE2 C:MET555 4.6 34.7 0.0 O C:VAL507 4.6 31.4 1.0 CA C:VAL486 4.7 41.3 1.0 HD11 C:ILE539 4.7 30.4 0.0 CG2 C:VAL486 4.8 42.9 1.0 N1 C:WIQ1004 4.8 54.0 1.0 HB3 C:MET555 4.8 25.1 0.0 O C:PHE483 4.8 50.5 1.0 C C:ALA506 4.8 30.5 1.0 CB C:PHE483 4.9 51.3 1.0 C3 C:WIQ1004 4.9 54.3 1.0 N C:VAL507 4.9 30.4 1.0 O C:ALA506 4.9 30.9 1.0 HD3 C:LYS508 5.0 40.8 0.0

J.S.Tyhonas, L.D.Arnold, J.M.Cox, A.Franovic, E.Gardiner, K.Grandinetti, R.Kania, T.Kanouni, M.Lardy, C.Li, E.S.Martin, N.Miller, A.Mohan, E.A.Murphy, M.Perez, L.Soroceanu, N.Timple, S.Uryu, S.Womble, S.W.Kaldor. Discovery of Kin-3248, An Irreversible, Next Generation Fgfr Inhibitor For the Treatment of Advanced Tumors Harboring FGFR2 and/or FGFR3 Gene Alterations. J.Med.Chem. 2024.
ISSN: ISSN 0022-2623
PubMed: 38267212
DOI: 10.1021/ACS.JMEDCHEM.3C01819