Sodium in PDB 4bvh: Crystal Structure of Human SIRT3 in Complex with the Inhibitor Ex-527 and 2'-O-Acetyl-Adp-Ribose

The structure of Crystal Structure of Human SIRT3 in Complex with the Inhibitor Ex-527 and 2'-O-Acetyl-Adp-Ribose, PDB code: 4bvh was solved by M.Gertz, M.Weyand, C.Steegborn, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.44 / 1.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	63.710, 66.530, 201.240, 90.00, 90.00, 90.00
R / Rfree (%)	17.159 / 22.581

The structure of Crystal Structure of Human SIRT3 in Complex with the Inhibitor Ex-527 and 2'-O-Acetyl-Adp-Ribose also contains other interesting chemical elements:

Zinc	(Zn)	3 atoms
Chlorine	(Cl)	5 atoms

The binding sites of Sodium atom in the Crystal Structure of Human SIRT3 in Complex with the Inhibitor Ex-527 and 2'-O-Acetyl-Adp-Ribose (pdb code 4bvh). 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 Crystal Structure of Human SIRT3 in Complex with the Inhibitor Ex-527 and 2'-O-Acetyl-Adp-Ribose, PDB code: 4bvh:

Sodium binding site 1 out of 1 in the Crystal Structure of Human SIRT3 in Complex with the Inhibitor Ex-527 and 2'-O-Acetyl-Adp-Ribose


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 Human SIRT3 in Complex with the Inhibitor Ex-527 and 2'-O-Acetyl-Adp-Ribose within 5.0Å range: probe atom residue distance (Å) B Occ A:Na1396 b:33.3 occ:1.00 OD2 A:ASP172 2.6 59.1 1.0 NE2 A:HIS187 2.8 57.4 1.0 CE1 A:HIS187 3.3 57.0 1.0 CG A:ASP172 3.7 56.2 1.0 CD2 A:HIS187 4.0 57.3 1.0 OD1 A:ASP172 4.1 54.8 1.0 ND1 A:HIS187 4.6 59.8 1.0 ND2 A:ASN188 4.7 50.8 1.0 CG A:HIS187 5.0 58.9 1.0

M.Gertz, F.Fischer, G.T.T.Nguyen, M.Lakshminarasimhan, M.Schutkowski, M.Weyand, C.Steegborn. Ex-527 Inhibits Sirtuins By Exploiting Their Unique Nad+-Dependent Deacetylation Mechanism Proc.Natl.Acad.Sci.Usa V. 110 E2772 2013.
ISSN: ISSN 0027-8424
PubMed: 23840057
DOI: 10.1073/PNAS.1303628110