Sodium in PDB 4jg6: RSK2 Ctd Bound to 2-Cyano-3-(1H-Indazol-5-Yl)Acrylamide

All present enzymatic activity of RSK2 Ctd Bound to 2-Cyano-3-(1H-Indazol-5-Yl)Acrylamide:
2.7.11.1;

The structure of RSK2 Ctd Bound to 2-Cyano-3-(1H-Indazol-5-Yl)Acrylamide, PDB code: 4jg6 was solved by R.M.Miller, V.O.Paavilainen, S.Krishnan, I.M.Serafimova, J.Taunton, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.67 / 2.60
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	47.280, 47.280, 291.970, 90.00, 90.00, 90.00
R / Rfree (%)	25.2 / 29.9

The binding sites of Sodium atom in the RSK2 Ctd Bound to 2-Cyano-3-(1H-Indazol-5-Yl)Acrylamide (pdb code 4jg6). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the RSK2 Ctd Bound to 2-Cyano-3-(1H-Indazol-5-Yl)Acrylamide, PDB code: 4jg6:

Sodium binding site 1 out of 1 in the RSK2 Ctd Bound to 2-Cyano-3-(1H-Indazol-5-Yl)Acrylamide


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of RSK2 Ctd Bound to 2-Cyano-3-(1H-Indazol-5-Yl)Acrylamide within 5.0Å range: probe atom residue distance (Å) B Occ A:Na802 b:44.1 occ:1.00 HG1 A:THR478 2.0 53.8 1.0 O A:ILE476 2.0 53.9 1.0 O A:HIS473 2.0 51.7 1.0 O A:HOH929 2.4 35.7 1.0 OG1 A:THR478 2.5 44.8 1.0 O A:GLY471 2.5 44.9 1.0 H A:ILE476 3.1 62.0 1.0 C A:ILE476 3.1 49.1 1.0 C A:HIS473 3.2 54.5 1.0 HB A:ILE476 3.5 65.6 1.0 C A:GLY471 3.6 55.5 1.0 HA A:THR478 3.6 56.7 1.0 N A:ILE476 3.7 51.7 1.0 CB A:THR478 3.7 46.6 1.0 CA A:ILE476 3.8 52.1 1.0 O A:PRO474 3.9 52.7 1.0 N A:THR478 3.9 44.4 1.0 HA A:PRO474 3.9 67.3 1.0 N A:HIS473 3.9 60.7 1.0 CA A:THR478 3.9 47.2 1.0 C A:PRO474 4.0 53.4 1.0 C A:GLN472 4.0 71.7 1.0 C A:ILE477 4.0 45.7 1.0 HA2 A:GLY471 4.1 61.1 1.0 N A:PRO474 4.1 56.9 1.0 CA A:HIS473 4.1 55.9 1.0 CB A:ILE476 4.1 54.7 1.0 O A:GLN472 4.1 73.0 1.0 H A:THR478 4.1 53.3 1.0 CA A:PRO474 4.2 56.1 1.0 HB3 A:HIS473 4.2 66.6 1.0 H A:HIS473 4.2 72.9 1.0 N A:ILE477 4.2 41.9 1.0 O A:ILE477 4.3 47.7 1.0 HG23 A:THR478 4.3 58.4 1.0 HD2 A:ARG558 4.3 52.8 1.0 HB A:THR478 4.4 56.0 1.0 HG22 A:ILE476 4.4 62.1 1.0 CA A:GLY471 4.4 50.9 1.0 HA A:ILE477 4.4 51.2 1.0 N A:GLN472 4.5 74.3 1.0 CA A:ILE477 4.5 42.6 1.0 OE2 A:GLU494 4.5 48.5 1.0 HA A:GLN472 4.5 95.7 1.0 CG2 A:THR478 4.5 48.6 1.0 N A:ASN475 4.6 49.0 1.0 CA A:GLN472 4.6 79.7 1.0 HE A:ARG558 4.7 55.2 1.0 CB A:HIS473 4.7 55.5 1.0 HA A:ILE476 4.7 62.6 1.0 C A:ASN475 4.8 49.2 1.0 HG21 A:THR478 4.8 58.4 1.0 CG2 A:ILE476 4.8 51.8 1.0 HA3 A:GLY471 4.9 61.1 1.0 H A:ASN475 4.9 58.8 1.0 HA A:HIS473 4.9 67.1 1.0 HD3 A:ARG558 4.9 52.8 1.0 CD A:ARG558 4.9 44.0 1.0 NE A:ARG558 5.0 46.0 1.0

R.M.Miller, V.O.Paavilainen, S.Krishnan, I.M.Serafimova, J.Taunton. Electrophilic Fragment-Based Design of Reversible Covalent Kinase Inhibitors. J.Am.Chem.Soc. V. 135 5298 2013.
ISSN: ISSN 0002-7863
PubMed: 23540679
DOI: 10.1021/JA401221B