Zinc in PDB 2h4j: SIR2-Deacetylated Peptide (From Enzymatic Turnover in Crystal)

The structure of SIR2-Deacetylated Peptide (From Enzymatic Turnover in Crystal), PDB code: 2h4j was solved by K.G.Hoff, J.L.Avalos, K.Sens, C.Wolberger, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	46.049, 59.683, 107.350, 90.00, 90.00, 90.00
R / Rfree (%)	19.8 / 24.6

The binding sites of Zinc atom in the SIR2-Deacetylated Peptide (From Enzymatic Turnover in Crystal) (pdb code 2h4j). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the SIR2-Deacetylated Peptide (From Enzymatic Turnover in Crystal), PDB code: 2h4j:

Zinc binding site 1 out of 1 in the SIR2-Deacetylated Peptide (From Enzymatic Turnover in Crystal)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of SIR2-Deacetylated Peptide (From Enzymatic Turnover in Crystal) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1001 b:35.0 occ:1.00 SG A:CYS127 2.2 33.5 1.0 SG A:CYS148 2.3 32.9 1.0 SG A:CYS124 2.4 26.9 1.0 SG A:CYS151 2.4 37.3 1.0 CB A:CYS148 3.1 34.5 1.0 CB A:CYS124 3.1 25.3 1.0 CB A:CYS127 3.4 31.9 1.0 CB A:CYS151 3.7 39.2 1.0 N A:CYS127 3.7 31.1 1.0 N A:CYS151 3.8 40.8 1.0 CA A:CYS127 4.1 32.3 1.0 CA A:CYS151 4.3 39.1 1.0 CB A:ASP150 4.5 41.5 1.0 CA A:CYS148 4.6 35.4 1.0 CA A:CYS124 4.6 25.0 1.0 CB A:LYS129 4.6 30.1 1.0 CB A:SER153 4.8 33.5 1.0 C A:CYS127 4.8 32.4 1.0 C A:CYS151 4.8 38.5 1.0 N A:GLU128 4.8 32.7 1.0 OG A:SER153 4.8 34.7 1.0 C A:ASP150 4.9 41.7 1.0 N A:SER153 4.9 34.2 1.0 CB A:ARG126 4.9 33.2 1.0 C A:ARG126 4.9 31.1 1.0 N A:ASN152 4.9 37.3 1.0 N A:LYS129 4.9 30.9 1.0 N A:ASP150 5.0 41.9 1.0

K.G.Hoff, J.L.Avalos, K.Sens, C.Wolberger. Insights Into the Sirtuin Mechanism From Ternary Complexes Containing Nad(+) and Acetylated Peptide. Structure V. 14 1231 2006.
ISSN: ISSN 0969-2126
PubMed: 16905097
DOI: 10.1016/J.STR.2006.06.006