Bromine in PDB 7yc3: Crystal Structure of FGFR4 Kinase Domain with 10T

All present enzymatic activity of Crystal Structure of FGFR4 Kinase Domain with 10T:
2.7.10.1;

The structure of Crystal Structure of FGFR4 Kinase Domain with 10T, PDB code: 7yc3 was solved by X.J.Chen, Q.M.Lin, Y.H.Chen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.76 / 1.99
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.333, 61.038, 60.516, 90, 98.01, 90
R / Rfree (%)	16.2 / 19.6

The binding sites of Bromine atom in the Crystal Structure of FGFR4 Kinase Domain with 10T (pdb code 7yc3). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total only one binding site of Bromine was determined in the Crystal Structure of FGFR4 Kinase Domain with 10T, PDB code: 7yc3:

Bromine binding site 1 out of 1 in the Crystal Structure of FGFR4 Kinase Domain with 10T


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Crystal Structure of FGFR4 Kinase Domain with 10T within 5.0Å range: probe atom residue distance (Å) B Occ A:Br801 b:46.9 occ:1.00 BRAW A:IIW801 0.0 46.9 1.0 CAB A:IIW801 2.0 27.3 1.0 CAA A:IIW801 2.9 23.7 1.0 CAC A:IIW801 2.9 26.6 1.0 CAJ A:IIW801 3.1 24.7 1.0 NH2 A:ARG483 3.3 36.3 1.0 OBH A:IIW801 3.6 23.4 1.0 CZ A:ARG483 3.9 39.8 1.0 NAF A:IIW801 4.2 22.3 1.0 CD A:ARG483 4.2 37.0 1.0 NE A:ARG483 4.2 39.2 1.0 CAD A:IIW801 4.2 26.6 1.0 O1 A:SO4803 4.2 56.0 1.0 CG2 A:THR499 4.3 27.6 1.0 O A:HOH1007 4.3 36.9 1.0 CB A:ALA554 4.3 22.0 1.0 CA A:ALA554 4.4 23.0 1.0 CAE A:IIW801 4.7 24.3 1.0 SG A:CYS552 4.7 29.4 1.0 CG A:ARG483 4.8 37.5 1.0 NH1 A:ARG483 4.9 38.8 1.0 O A:ALA554 4.9 21.9 1.0

F.Yang, X.Chen, X.Song, R.Ortega, X.Lin, W.Deng, J.Guo, Z.Tu, A.V.Patterson, J.B.Smaill, Y.Chen, X.Lu. Design, Synthesis, and Biological Evaluation of 5-Formyl-Pyrrolo[3,2- B ]Pyridine-3-Carboxamides As New Selective, Potent, and Reversible-Covalent FGFR4 Inhibitors. J.Med.Chem. V. 65 14809 2022.
ISSN: ISSN 0022-2623
PubMed: 36278929
DOI: 10.1021/ACS.JMEDCHEM.2C01319