Chlorine in PDB 5jkg: The Crystal Structure of FGFR4 Kinase Domain in Complex with LY2874455

All present enzymatic activity of The Crystal Structure of FGFR4 Kinase Domain in Complex with LY2874455:
2.7.10.1;

The structure of The Crystal Structure of FGFR4 Kinase Domain in Complex with LY2874455, PDB code: 5jkg was solved by D.Wu, L.Chen, Y.Chen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	31.89 / 2.35
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	61.887, 61.887, 186.059, 90.00, 90.00, 90.00
R / Rfree (%)	23.3 / 27.7

The binding sites of Chlorine atom in the The Crystal Structure of FGFR4 Kinase Domain in Complex with LY2874455 (pdb code 5jkg). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the The Crystal Structure of FGFR4 Kinase Domain in Complex with LY2874455, PDB code: 5jkg:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the The Crystal Structure of FGFR4 Kinase Domain in Complex with LY2874455


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of The Crystal Structure of FGFR4 Kinase Domain in Complex with LY2874455 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl801 b:84.5 occ:1.00 CL1 A:6LF801 0.0 84.5 1.0 CAY A:6LF801 1.8 78.1 1.0 CBC A:6LF801 2.7 76.4 1.0 CAP A:6LF801 2.8 73.3 1.0 OAC A:6LF801 2.9 58.9 1.0 CAK A:6LF801 3.2 68.6 1.0 CAS A:6LF801 3.5 69.0 1.0 CAM A:6LF801 3.7 53.2 1.0 CB A:ALA629 3.8 49.5 1.0 NAI A:6LF801 4.0 77.2 1.0 CAZ A:6LF801 4.1 78.5 1.0 CAR A:6LF801 4.3 50.8 1.0 CAO A:6LF801 4.5 54.1 1.0 CBD A:6LF801 4.5 74.5 1.0 OD2 A:ASP630 4.5 93.3 1.0 OE1 A:GLU475 4.7 0.8 1.0 CD1 A:LEU619 4.8 45.8 1.0 O A:ARG616 4.9 49.3 1.0

Chlorine binding site 2 out of 2 in the The Crystal Structure of FGFR4 Kinase Domain in Complex with LY2874455


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of The Crystal Structure of FGFR4 Kinase Domain in Complex with LY2874455 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl801 b:94.9 occ:1.00 CL2 A:6LF801 0.0 94.9 1.0 CAZ A:6LF801 1.8 78.5 1.0 CAP A:6LF801 2.7 73.3 1.0 CBD A:6LF801 2.7 74.5 1.0 O A:LEU473 3.0 76.5 1.0 CAK A:6LF801 3.0 68.6 1.0 CBA A:6LF801 3.4 57.4 1.0 CAV A:6LF801 3.5 51.0 1.0 C A:LEU473 3.6 70.1 1.0 CAS A:6LF801 3.7 69.0 1.0 CAU A:6LF801 3.9 56.8 1.0 CAO A:6LF801 3.9 54.1 1.0 NAI A:6LF801 4.0 77.2 1.0 CA A:GLY474 4.0 85.1 1.0 CAY A:6LF801 4.0 78.1 1.0 N A:GLY474 4.0 74.7 1.0 CB A:LEU473 4.2 59.7 1.0 OAC A:6LF801 4.2 58.9 1.0 CA A:LEU473 4.5 62.0 1.0 CBC A:6LF801 4.5 76.4 1.0 CAM A:6LF801 4.6 53.2 1.0 NAH A:6LF801 4.6 64.2 1.0 OE2 A:GLU475 4.7 0.5 1.0 C A:GLY474 4.9 94.9 1.0 CAT A:6LF801 5.0 50.2 1.0 CAJ A:6LF801 5.0 48.6 1.0

D.Wu, M.Guo, M.A.Philips, L.Qu, L.Jiang, J.Li, X.Chen, Z.Chen, L.Chen, Y.Chen. Crystal Structure of the FGFR4/LY2874455 Complex Reveals Insights Into the Pan-Fgfr Selectivity of LY2874455 Plos One V. 11 62491 2016.
ISSN: ESSN 1932-6203
PubMed: 27618313
DOI: 10.1371/JOURNAL.PONE.0162491