Chlorine in PDB 4buz: SIR2 Complex Structure Mixture of Ex-527 Inhibitor and Reaction Products or of Reaction Substrates P53 Peptide and Nad

The structure of SIR2 Complex Structure Mixture of Ex-527 Inhibitor and Reaction Products or of Reaction Substrates P53 Peptide and Nad, PDB code: 4buz was solved by M.Weyand, M.Lakshminarasimhan, M.Gertz, C.Steegborn, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.32 / 1.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	46.750, 59.920, 109.030, 90.00, 90.00, 90.00
R / Rfree (%)	15.93 / 19.357

The structure of SIR2 Complex Structure Mixture of Ex-527 Inhibitor and Reaction Products or of Reaction Substrates P53 Peptide and Nad also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Chlorine atom in the SIR2 Complex Structure Mixture of Ex-527 Inhibitor and Reaction Products or of Reaction Substrates P53 Peptide and Nad (pdb code 4buz). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the SIR2 Complex Structure Mixture of Ex-527 Inhibitor and Reaction Products or of Reaction Substrates P53 Peptide and Nad, PDB code: 4buz:

Chlorine binding site 1 out of 1 in the SIR2 Complex Structure Mixture of Ex-527 Inhibitor and Reaction Products or of Reaction Substrates P53 Peptide and Nad


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of SIR2 Complex Structure Mixture of Ex-527 Inhibitor and Reaction Products or of Reaction Substrates P53 Peptide and Nad within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1247 b:29.4 occ:0.60 CL A:OCZ1247 0.0 29.4 0.6 CAB A:OCZ1247 1.8 27.8 0.6 CD1 A:PHE48 2.5 33.1 1.0 CH3 P:ALY382 2.6 23.9 0.4 CG2 A:ILE159 2.6 16.2 0.4 CAC A:OCZ1247 2.7 26.8 0.6 CAA A:OCZ1247 2.8 29.9 0.6 CE1 A:PHE48 2.8 38.8 1.0 C7D A:OAD1249 3.4 52.2 0.6 CD1 A:ILE159 3.4 20.4 0.6 CG A:PHE48 3.5 33.7 1.0 O A:VAL160 3.6 17.4 1.0 O6D A:OAD1249 3.6 52.2 0.6 CH P:ALY382 3.7 26.1 0.4 CG1 A:ILE159 3.8 18.7 0.6 C6D A:OAD1249 3.8 47.9 0.6 CZ A:PHE48 3.9 37.6 1.0 NZ P:ALY382 4.0 30.0 1.0 CAD A:OCZ1247 4.0 28.7 0.6 CB A:ILE159 4.1 17.8 0.6 CAF A:OCZ1247 4.1 26.4 0.6 CB A:ILE159 4.1 15.8 0.4 CB A:PHE48 4.1 29.5 1.0 C A:VAL160 4.3 17.5 1.0 CD2 A:PHE48 4.4 38.7 1.0 CA A:PHE161 4.5 18.4 1.0 CAE A:OCZ1247 4.5 26.8 0.6 CE2 A:PHE48 4.6 38.4 1.0 OH P:ALY382 4.6 21.4 0.4 N A:PHE161 4.7 18.5 1.0 CD1 A:ILE159 4.7 14.3 0.4 CG1 A:ILE159 4.8 15.0 0.4 CD2 A:PHE161 4.9 21.2 1.0 CG2 A:ILE159 4.9 17.6 0.6 N A:VAL160 4.9 18.4 1.0 CA A:PHE48 4.9 26.0 1.0 O A:PHE48 5.0 26.9 1.0 O2D A:OAD1249 5.0 45.8 0.6

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