Sodium in PDB 8g1q: Co-Crystal Structure of Compound 1 in Complex with the Bromodomain of Human SMARCA4 and Pvhl:Elonginc:Elonginb

The structure of Co-Crystal Structure of Compound 1 in Complex with the Bromodomain of Human SMARCA4 and Pvhl:Elonginc:Elonginb, PDB code: 8g1q was solved by S.Ghimire Rijal, R.P.Wurz, A.Vaish, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.66 / 3.73
Space group	P 62
Cell size a, b, c (Å), α, β, γ (°)	158.163, 158.163, 44.857, 90, 90, 120
R / Rfree (%)	23.5 / 32.6

The binding sites of Sodium atom in the Co-Crystal Structure of Compound 1 in Complex with the Bromodomain of Human SMARCA4 and Pvhl:Elonginc:Elonginb (pdb code 8g1q). 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 Co-Crystal Structure of Compound 1 in Complex with the Bromodomain of Human SMARCA4 and Pvhl:Elonginc:Elonginb, PDB code: 8g1q:

Sodium binding site 1 out of 1 in the Co-Crystal Structure of Compound 1 in Complex with the Bromodomain of Human SMARCA4 and Pvhl:Elonginc:Elonginb


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Co-Crystal Structure of Compound 1 in Complex with the Bromodomain of Human SMARCA4 and Pvhl:Elonginc:Elonginb within 5.0Å range: probe atom residue distance (Å) B Occ H:Na1601 b:38.5 occ:1.00 O H:GLU1483 3.4 49.8 1.0 C04 C:YHB301 3.5 60.7 1.0 O1 C:PEG302 3.6 57.5 1.0 C17 C:YHB301 3.7 59.8 1.0 N H:GLN1487 3.9 53.1 1.0 CB H:ILE1486 4.0 48.2 1.0 O21 C:YHB301 4.0 51.4 1.0 C1 C:PEG302 4.1 58.3 1.0 N03 C:YHB301 4.2 59.4 1.0 O01 C:YHB301 4.2 54.3 1.0 CB H:GLN1487 4.3 60.9 1.0 CG2 H:ILE1486 4.4 53.6 1.0 O H:GLN1487 4.4 49.0 1.0 C02 C:YHB301 4.6 55.6 1.0 CA H:GLN1487 4.6 54.5 1.0 C H:GLU1483 4.6 48.2 1.0 C05 C:YHB301 4.6 63.9 1.0 CA H:ILE1486 4.8 42.8 1.0 C H:ILE1486 4.9 47.7 1.0 CG1 H:ILE1486 4.9 56.2 1.0 C16 C:YHB301 4.9 61.9 1.0 N H:ILE1486 5.0 42.5 1.0

R.P.Wurz, H.Rui, K.Dellamaggiore, S.Ghimire-Rijal, K.Choi, K.Smither, A.Amegadzie, N.Chen, X.Li, A.Banerjee, Q.Chen, D.Mohl, A.Vaish. Affinity and Cooperativity Modulate Ternary Complex Formation to Drive Targeted Protein Degradation. Nat Commun V. 14 4177 2023.
ISSN: ESSN 2041-1723
PubMed: 37443112
DOI: 10.1038/S41467-023-39904-5