Sodium in PDB 5lv2: Crystal Structure of Mouse CARM1 in Complex with Inhibitor LH1246

All present enzymatic activity of Crystal Structure of Mouse CARM1 in Complex with Inhibitor LH1246:
2.1.1.319;

The structure of Crystal Structure of Mouse CARM1 in Complex with Inhibitor LH1246, PDB code: 5lv2 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)	49.34 / 2.29
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	98.684, 74.832, 206.639, 90.00, 90.53, 90.00
R / Rfree (%)	20.5 / 23.8

The binding sites of Sodium atom in the Crystal Structure of Mouse CARM1 in Complex with Inhibitor LH1246 (pdb code 5lv2). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Crystal Structure of Mouse CARM1 in Complex with Inhibitor LH1246, PDB code: 5lv2:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in the Crystal Structure of Mouse CARM1 in Complex with Inhibitor LH1246


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of Mouse CARM1 in Complex with Inhibitor LH1246 within 5.0Å range: probe atom residue distance (Å) B Occ D:Na505 b:38.1 occ:1.00 O D:ALA408 2.6 31.5 1.0 HA D:THR407 2.8 29.0 1.0 O D:HOH661 2.8 23.4 1.0 O D:PRO412 2.9 33.4 1.0 C D:THR407 3.1 25.3 1.0 HE22 D:GLN418 3.1 37.7 1.0 HB2 D:GLU411 3.1 40.4 1.0 HA D:LEU413 3.2 34.4 1.0 O D:THR407 3.2 24.6 1.0 HE21 D:GLN418 3.2 37.7 1.0 HG23 D:THR414 3.3 31.9 1.0 O D:GLU411 3.3 29.0 1.0 O D:HOH644 3.3 25.3 1.0 CA D:THR407 3.4 24.2 1.0 NE2 D:GLN418 3.5 31.4 1.0 C D:ALA408 3.5 28.8 1.0 N D:ALA408 3.6 28.5 1.0 H D:THR414 3.6 37.8 1.0 C D:PRO412 3.7 32.6 1.0 C D:GLU411 3.8 30.1 1.0 H D:ALA408 3.9 34.2 1.0 CA D:LEU413 3.9 28.7 1.0 CB D:GLU411 4.0 33.6 1.0 H D:GLU411 4.0 40.2 1.0 O D:SER406 4.0 27.5 1.0 O D:HOH647 4.0 25.9 1.0 HD12 D:LEU413 4.1 50.7 1.0 HG1 D:THR414 4.1 34.4 1.0 N D:THR414 4.1 31.5 1.0 N D:LEU413 4.2 28.2 1.0 CA D:ALA408 4.2 28.7 1.0 HB3 D:GLU411 4.2 40.4 1.0 HA D:PRO409 4.2 35.0 1.0 HB D:THR407 4.2 24.5 1.0 CG2 D:THR414 4.2 26.6 1.0 CA D:GLU411 4.3 32.8 1.0 N D:THR407 4.4 22.3 1.0 C D:LEU413 4.4 31.0 1.0 CB D:THR407 4.4 20.4 1.0 N D:PRO412 4.5 30.6 1.0 HG21 D:THR414 4.5 31.9 1.0 N D:PRO409 4.5 29.1 1.0 C D:SER406 4.5 26.1 1.0 N D:GLU411 4.5 33.5 1.0 CA D:PRO412 4.7 31.2 1.0 HG22 D:THR414 4.7 31.9 1.0 HA D:ALA408 4.8 34.4 1.0 CA D:PRO409 4.8 29.1 1.0 OG1 D:THR414 4.8 28.7 1.0 CD D:GLN418 4.8 32.0 1.0 H D:LEU413 4.9 33.9 1.0 CD1 D:LEU413 4.9 42.2 1.0 HG22 D:THR407 4.9 24.2 1.0 CB D:THR414 5.0 28.1 1.0

Sodium binding site 2 out of 2 in the Crystal Structure of Mouse CARM1 in Complex with Inhibitor LH1246


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of Crystal Structure of Mouse CARM1 in Complex with Inhibitor LH1246 within 5.0Å range: probe atom residue distance (Å) B Occ F:Na506 b:33.7 occ:1.00 O F:PRO412 2.7 33.3 1.0 HA F:THR407 2.8 31.2 1.0 O F:ALA408 2.8 26.6 1.0 O F:HOH656 2.8 28.1 1.0 HA F:LEU413 3.0 37.6 1.0 HG23 F:THR414 3.1 35.3 1.0 HE22 F:GLN418 3.2 37.9 1.0 C F:THR407 3.3 27.3 1.0 O F:GLU411 3.3 26.8 1.0 HB2 F:GLU411 3.3 39.9 1.0 HE21 F:GLN418 3.3 37.9 1.0 O F:HOH665 3.3 25.6 1.0 O F:THR407 3.4 28.5 1.0 H F:THR414 3.4 37.1 1.0 CA F:THR407 3.5 26.0 1.0 C F:PRO412 3.5 34.4 1.0 NE2 F:GLN418 3.6 31.6 1.0 N F:ALA408 3.7 28.1 1.0 C F:ALA408 3.7 28.0 1.0 O F:HOH615 3.8 36.5 1.0 CA F:LEU413 3.8 31.3 1.0 C F:GLU411 3.8 29.9 1.0 HD12 F:LEU413 3.8 40.0 1.0 N F:THR414 3.9 30.9 1.0 O F:SER406 4.0 29.7 1.0 N F:LEU413 4.0 33.0 1.0 HG1 F:THR414 4.0 35.1 1.0 H F:ALA408 4.1 33.7 1.0 CG2 F:THR414 4.1 29.4 1.0 CB F:GLU411 4.1 33.3 1.0 C F:LEU413 4.2 32.9 1.0 H F:GLU411 4.2 41.5 1.0 HB F:THR407 4.3 28.4 1.0 HB3 F:GLU411 4.3 39.9 1.0 HA F:PRO409 4.3 35.1 1.0 CA F:ALA408 4.4 28.4 1.0 N F:PRO412 4.4 32.4 1.0 HG21 F:THR414 4.4 35.3 1.0 CA F:GLU411 4.4 32.2 1.0 N F:THR407 4.4 25.5 1.0 CB F:THR407 4.5 23.7 1.0 CA F:PRO412 4.5 32.2 1.0 C F:SER406 4.6 26.9 1.0 HG22 F:THR414 4.6 35.3 1.0 N F:PRO409 4.7 29.0 1.0 OG1 F:THR414 4.7 29.3 1.0 CD1 F:LEU413 4.7 33.4 1.0 N F:GLU411 4.7 34.6 1.0 H F:LEU413 4.8 39.5 1.0 HG22 F:THR407 4.8 27.1 1.0 CB F:THR414 4.8 30.1 1.0 HD13 F:LEU413 4.9 40.0 1.0 CA F:PRO409 4.9 29.2 1.0 CD F:GLN418 5.0 32.7 1.0 HA F:ALA408 5.0 34.1 1.0 CA F:THR414 5.0 28.7 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.Lond.B V. 373 2018BIOL.Sci..
ISSN: ESSN 1471-2970
PubMed: 29685976
DOI: 10.1098/RSTB.2017.0072