Fluorine in PDB 6ocq: Crystal Structure of RIP1 Kinase in Complex with A Pyrrolidine

All present enzymatic activity of Crystal Structure of RIP1 Kinase in Complex with A Pyrrolidine:
2.7.11.1;

The structure of Crystal Structure of RIP1 Kinase in Complex with A Pyrrolidine, PDB code: 6ocq was solved by J.H.Thorpe, P.A.Harris, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	76.18 / 2.79
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	47.297, 95.117, 127.240, 90.00, 90.00, 90.00
R / Rfree (%)	20.3 / 26.8

The binding sites of Fluorine atom in the Crystal Structure of RIP1 Kinase in Complex with A Pyrrolidine (pdb code 6ocq). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Crystal Structure of RIP1 Kinase in Complex with A Pyrrolidine, PDB code: 6ocq:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Crystal Structure of RIP1 Kinase in Complex with A Pyrrolidine


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 RIP1 Kinase in Complex with A Pyrrolidine within 5.0Å range: probe atom residue distance (Å) B Occ A:F301 b:71.7 occ:1.00 F18 A:M5J301 0.0 71.7 1.0 C6 A:M5J301 1.4 63.0 1.0 C3 A:M5J301 2.3 59.5 1.0 C4 A:M5J301 2.4 57.5 1.0 OD2 A:ASP156 3.5 72.4 1.0 OG A:SER161 3.5 68.5 1.0 C1 A:M5J301 3.6 55.5 1.0 C5 A:M5J301 3.6 53.6 1.0 CG1 A:VAL134 3.7 52.6 1.0 CB A:ASP156 3.7 59.7 1.0 CE2 A:PHE162 3.8 67.2 1.0 CB A:SER161 3.9 70.2 1.0 CG A:ASP156 4.1 69.2 1.0 C2 A:M5J301 4.1 56.9 1.0 CZ A:PHE162 4.3 68.4 1.0 CD1 A:LEU70 4.5 56.3 1.0 CD2 A:HIS136 4.8 54.5 1.0 CD2 A:PHE162 4.8 73.9 1.0 C11 A:M5J301 4.9 51.4 1.0

Fluorine binding site 2 out of 2 in the Crystal Structure of RIP1 Kinase in Complex with A Pyrrolidine


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 RIP1 Kinase in Complex with A Pyrrolidine within 5.0Å range: probe atom residue distance (Å) B Occ B:F301 b:69.8 occ:1.00 F18 B:M5J301 0.0 69.8 1.0 C6 B:M5J301 1.3 63.0 1.0 C3 B:M5J301 2.3 59.1 1.0 C4 B:M5J301 2.3 55.7 1.0 CE2 B:PHE162 3.4 79.1 1.0 C5 B:M5J301 3.6 55.5 1.0 C1 B:M5J301 3.6 52.4 1.0 CZ B:PHE162 3.7 76.4 1.0 CB B:ASP156 3.8 64.8 1.0 OD2 B:ASP156 4.0 75.5 1.0 CG1 B:VAL134 4.0 55.8 1.0 C2 B:M5J301 4.0 54.9 1.0 CD1 B:LEU70 4.2 60.8 1.0 CB B:SER161 4.2 78.2 1.0 CG B:ASP156 4.4 77.4 1.0 CD2 B:PHE162 4.5 75.5 1.0 OG B:SER161 4.7 93.5 1.0 C11 B:M5J301 4.8 60.8 1.0 CE1 B:PHE162 4.8 79.5 1.0 CD2 B:LEU129 4.9 49.2 1.0

P.A.Harris, N.Faucher, N.George, P.M.Eidam, B.W.King, G.V.White, N.A.Anderson, D.Bandyopadhyay, A.M.Beal, V.Beneton, S.B.Berger, N.Campobasso, S.Campos, C.A.Capriotti, J.A.Cox, A.Daugan, F.Donche, M.H.Fouchet, J.N.Finger, B.Geddes, P.J.Gough, P.Grondin, B.L.Hoffman, S.J.Hoffman, S.E.Hutchinson, J.U.Jeong, E.Jigorel, P.Lamoureux, L.K.Leister, J.D.Lich, M.K.Mahajan, J.Meslamani, J.E.Mosley, R.Nagilla, P.M.Nassau, S.L.Ng, M.T.Ouellette, K.K.Pasikanti, F.Potvain, M.A.Reilly, E.J.Rivera, S.Sautet, M.C.Schaeffer, C.A.Sehon, H.Sun, J.H.Thorpe, R.D.Totoritis, P.Ward, N.Wellaway, D.D.Wisnoski, J.M.Woolven, J.Bertin, R.W.Marquis. Discovery and Lead-Optimization of 4,5-Dihydropyrazoles As Mono-Kinase Selective, Orally Bioavailable and Efficacious Inhibitors of Receptor Interacting Protein 1 (RIP1) Kinase. J.Med.Chem. V. 62 5096 2019.
ISSN: ISSN 0022-2623
PubMed: 31013427
DOI: 10.1021/ACS.JMEDCHEM.9B00318