Bromine in PDB 4er7: Crystal Structure of Human DOT1L in Complex with Inhibitor SGC0947

All present enzymatic activity of Crystal Structure of Human DOT1L in Complex with Inhibitor SGC0947:
2.1.1.43;

The structure of Crystal Structure of Human DOT1L in Complex with Inhibitor SGC0947, PDB code: 4er7 was solved by A.K.Wernimont, W.Tempel, W.Yu, A.Scopton, Y.Li, K.T.Nguyen, M.Vedadi, J.E.Bradner, M.Schapira, C.H.Arrowsmith, A.M.Edwards, C.Bountra, P.J.Brown, Structural Genomics Consortium (Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.00 / 2.20
Space group	P 65
Cell size a, b, c (Å), α, β, γ (°)	150.617, 150.617, 52.800, 90.00, 90.00, 120.00
R / Rfree (%)	21.8 / 24.2

The binding sites of Bromine atom in the Crystal Structure of Human DOT1L in Complex with Inhibitor SGC0947 (pdb code 4er7). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 2 binding sites of Bromine where determined in the Crystal Structure of Human DOT1L in Complex with Inhibitor SGC0947, PDB code: 4er7:
Jump to Bromine binding site number: 1; 2;

Bromine binding site 1 out of 2 in the Crystal Structure of Human DOT1L in Complex with Inhibitor SGC0947


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 Human DOT1L in Complex with Inhibitor SGC0947 within 5.0Å range: probe atom residue distance (Å) B Occ A:Br501 b:54.9 occ:0.50 BRH A:AW3501 0.0 54.9 0.5 N1 A:AW3501 0.8 53.6 0.3 C6 A:AW3501 1.5 52.9 0.3 C2 A:AW3501 1.7 53.0 0.3 CBB A:AW3501 1.9 48.7 0.7 NAD A:AW3501 2.4 52.0 0.3 C5 A:AW3501 2.5 52.9 0.3 N3 A:AW3501 2.7 52.3 0.3 CAN A:AW3501 2.9 47.5 0.7 C5 A:AW3501 2.9 47.4 0.7 C4 A:AW3501 2.9 52.2 0.3 NAD A:AW3501 3.0 46.6 0.7 C6 A:AW3501 3.4 46.3 0.7 CBB A:AW3501 3.7 53.1 0.3 NBJ A:AW3501 4.0 48.1 0.7 CZ A:PHE223 4.0 45.7 1.0 C4 A:AW3501 4.0 46.7 0.7 CG1 A:VAL249 4.0 47.0 1.0 CG2 A:VAL249 4.2 48.2 1.0 NBJ A:AW3501 4.2 51.9 0.3 CZ A:PHE245 4.5 48.5 1.0 CE1 A:PHE245 4.6 49.7 1.0 CAN A:AW3501 4.6 52.4 0.3 CE2 A:PHE223 4.7 43.6 1.0 CE1 A:PHE223 4.7 44.0 1.0 BRH A:AW3501 4.7 56.5 0.2 CB A:VAL249 4.7 48.5 1.0 N1 A:AW3501 4.8 47.4 0.7 CE2 A:PHE245 4.8 48.6 1.0 CD1 A:PHE245 4.9 50.2 1.0

Bromine binding site 2 out of 2 in the Crystal Structure of Human DOT1L in Complex with Inhibitor SGC0947


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Crystal Structure of Human DOT1L in Complex with Inhibitor SGC0947 within 5.0Å range: probe atom residue distance (Å) B Occ A:Br501 b:56.5 occ:0.20 BRH A:AW3501 0.0 56.5 0.2 N1 A:AW3501 0.3 47.4 0.7 C6 A:AW3501 1.3 46.3 0.7 C2 A:AW3501 1.7 44.2 0.7 CBB A:AW3501 1.9 53.1 0.3 NAD A:AW3501 2.1 46.6 0.7 C5 A:AW3501 2.4 47.4 0.7 N3 A:AW3501 2.7 43.0 0.7 C5 A:AW3501 2.9 52.9 0.3 CAN A:AW3501 2.9 52.4 0.3 NAD A:AW3501 2.9 52.0 0.3 C4 A:AW3501 2.9 46.7 0.7 OD1 A:ASP222 3.1 59.5 1.0 N A:PHE223 3.1 53.3 1.0 CD2 A:PHE223 3.2 43.7 1.0 C6 A:AW3501 3.3 52.9 0.3 CE2 A:PHE223 3.4 43.6 1.0 CA A:ASP222 3.6 55.4 1.0 CG A:PHE223 3.6 48.3 1.0 CBB A:AW3501 3.7 48.7 0.7 C A:ASP222 3.8 54.3 1.0 CG A:ASP222 3.9 57.9 1.0 CZ A:PHE223 4.0 45.7 1.0 C4 A:AW3501 4.0 52.2 0.3 NBJ A:AW3501 4.0 51.9 0.3 O A:GLY221 4.0 55.1 1.0 CB A:LYS187 4.0 52.0 1.0 CD1 A:PHE223 4.1 44.8 1.0 CA A:PHE223 4.2 52.3 1.0 NBJ A:AW3501 4.2 48.1 0.7 CG A:LYS187 4.2 53.0 1.0 CB A:PHE223 4.2 51.1 1.0 CE1 A:PHE223 4.3 44.0 1.0 CD A:LYS187 4.3 53.2 1.0 CB A:ASP222 4.3 56.1 1.0 CAN A:AW3501 4.5 47.5 0.7 N A:LEU224 4.6 53.2 1.0 N A:ASP222 4.6 54.9 1.0 N A:LYS187 4.7 50.8 1.0 N1 A:AW3501 4.7 53.6 0.3 C A:GLY221 4.7 54.8 1.0 BRH A:AW3501 4.7 54.9 0.5 OD2 A:ASP222 4.8 61.0 1.0 C A:PHE223 4.9 52.8 1.0 CA A:LYS187 4.9 52.2 1.0

W.Yu, E.J.Chory, A.K.Wernimont, W.Tempel, A.Scopton, A.Federation, J.J.Marineau, J.Qi, D.Barsyte-Lovejoy, J.Yi, R.Marcellus, R.E.Iacob, J.R.Engen, C.Griffin, A.Aman, E.Wienholds, F.Li, J.Pineda, G.Estiu, T.Shatseva, T.Hajian, R.Al-Awar, J.E.Dick, M.Vedadi, P.J.Brown, C.H.Arrowsmith, J.E.Bradner, M.Schapira. Catalytic Site Remodelling of the DOT1L Methyltransferase By Selective Inhibitors. Nat Commun V. 3 1288 2012.
ISSN: ESSN 2041-1723
PubMed: 23250418
DOI: 10.1038/NCOMMS2304