Bromine in PDB 5lv3: Crystal Structure of Mouse CARM1 in Complex with Ligand LH1561BR

All present enzymatic activity of Crystal Structure of Mouse CARM1 in Complex with Ligand LH1561BR:
2.1.1.319;

The structure of Crystal Structure of Mouse CARM1 in Complex with Ligand LH1561BR, PDB code: 5lv3 was solved by V.Cura, N.Marechal, N.Troffer-Charlier, L.Halby, P.Arimondo, L.Bonnefond, J.Cavarelli, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.99 / 1.80
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	75.092, 98.524, 208.097, 90.00, 90.00, 90.00
R / Rfree (%)	17.4 / 20.3

The binding sites of Bromine atom in the Crystal Structure of Mouse CARM1 in Complex with Ligand LH1561BR (pdb code 5lv3). 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 Mouse CARM1 in Complex with Ligand LH1561BR, PDB code: 5lv3:
Jump to Bromine binding site number: 1; 2;

Bromine binding site 1 out of 2 in the Crystal Structure of Mouse CARM1 in Complex with Ligand LH1561BR


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 Mouse CARM1 in Complex with Ligand LH1561BR within 5.0Å range: probe atom residue distance (Å) B Occ B:Br501 b:0.1 occ:1.00 BR1 B:LHF501 0.0 0.1 1.0 C54 B:LHF501 1.9 96.5 1.0 C59 B:LHF501 2.8 92.8 1.0 C55 B:LHF501 2.8 90.9 1.0 H61 B:LHF501 2.9 0.0 1.0 H64 B:LHF501 2.9 0.4 1.0 HA B:TYR150 3.1 27.3 1.0 HD1 B:TYR150 3.2 23.4 1.0 O B:HOH615 3.4 25.5 1.0 HE3 B:LYS471 3.5 45.6 1.0 HG2 B:GLN149 3.5 69.7 1.0 HB2 B:TYR150 3.9 25.6 1.0 CA B:TYR150 4.0 22.8 1.0 CD1 B:TYR150 4.0 19.5 1.0 HE2 B:LYS471 4.0 45.6 1.0 C56 B:LHF501 4.1 87.6 1.0 C58 B:LHF501 4.1 90.8 1.0 CE B:LYS471 4.2 38.0 1.0 CB B:TYR150 4.3 21.3 1.0 CG B:GLN149 4.4 58.1 1.0 HB2 B:PHE153 4.4 30.4 1.0 HE21 B:GLN149 4.5 90.9 1.0 HB3 B:PHE153 4.5 30.4 1.0 HZ1 B:LYS471 4.5 49.4 1.0 N B:TYR150 4.5 21.2 1.0 HG3 B:GLN149 4.5 69.7 1.0 CG B:TYR150 4.6 18.8 1.0 C57 B:LHF501 4.6 86.1 1.0 NE2 B:GLN149 4.7 75.7 1.0 CD B:GLN149 4.7 73.2 1.0 O B:GLN149 4.7 20.9 1.0 C B:GLN149 4.8 26.4 1.0 CB B:PHE153 4.8 25.3 1.0 NZ B:LYS471 4.9 41.2 1.0 H B:TYR150 4.9 25.4 1.0 HE1 B:TYR150 4.9 23.3 1.0 H63 B:LHF501 4.9 1.0 1.0 CE1 B:TYR150 4.9 19.4 1.0 H62 B:LHF501 5.0 0.1 1.0

Bromine binding site 2 out of 2 in the Crystal Structure of Mouse CARM1 in Complex with Ligand LH1561BR


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 Mouse CARM1 in Complex with Ligand LH1561BR within 5.0Å range: probe atom residue distance (Å) B Occ C:Br501 b:80.2 occ:1.00 BR1 C:LHF501 0.0 80.2 1.0 C54 C:LHF501 1.9 81.5 1.0 C55 C:LHF501 2.8 77.4 1.0 C59 C:LHF501 2.8 82.3 1.0 H61 C:LHF501 2.9 92.9 1.0 H64 C:LHF501 2.9 98.7 1.0 HD1 C:TYR150 3.1 33.2 1.0 HE3 C:LYS471 3.2 44.4 1.0 O C:HOH620 3.2 23.4 1.0 HA C:TYR150 3.4 30.7 1.0 HE21 C:GLN149 3.5 0.5 1.0 HE2 C:LYS471 3.5 44.4 1.0 HG2 C:GLN149 3.7 94.9 1.0 CE C:LYS471 3.8 37.0 1.0 NE2 C:GLN149 4.0 0.4 1.0 CD1 C:TYR150 4.0 27.6 1.0 HB2 C:TYR150 4.0 27.4 1.0 C56 C:LHF501 4.1 77.1 1.0 C58 C:LHF501 4.1 82.4 1.0 HZ1 C:LYS471 4.2 38.6 1.0 CA C:TYR150 4.3 25.6 1.0 HE22 C:GLN149 4.3 0.5 1.0 O C:HOH607 4.3 46.0 1.0 CB C:TYR150 4.5 22.8 1.0 CG C:GLN149 4.5 79.1 1.0 CD C:GLN149 4.5 97.1 1.0 NZ C:LYS471 4.5 32.2 1.0 C57 C:LHF501 4.6 80.2 1.0 N C:TYR150 4.7 20.9 1.0 CG C:TYR150 4.8 22.2 1.0 HE1 C:TYR150 4.8 32.6 1.0 HD2 C:LYS471 4.8 38.1 1.0 CE1 C:TYR150 4.9 27.1 1.0 H C:TYR150 4.9 25.1 1.0 H63 C:LHF501 4.9 98.8 1.0 HG2 C:GLU267 5.0 28.1 1.0 H62 C:LHF501 5.0 92.5 1.0 CD C:LYS471 5.0 31.7 1.0 HZ2 C:LYS471 5.0 38.6 1.0

L.Halby, N.Marechal, D.Pechalrieu, V.Cura, D.M.Franchini, C.Faux, F.Alby, N.Troffer-Charlier, S.Kudithipudi, A.Jeltsch, W.Aouadi, E.Decroly, J.C.Guillemot, P.Page, C.Ferroud, L.Bonnefond, D.Guianvarc'h, J.Cavarelli, P.B.Arimondo. Hijacking Dna Methyltransferase Transition State Analogues to Produce Chemical Scaffolds For Prmt Inhibitors. Philos. Trans. R. Soc. V. 373 2018LOND., B, Biol. Sci..
ISSN: ESSN 1471-2970
PubMed: 29685976
DOI: 10.1098/RSTB.2017.0072