Zinc in PDB 1ma3: Structure of A SIR2 Enzyme Bound to An Acetylated P53 Peptide

The structure of Structure of A SIR2 Enzyme Bound to An Acetylated P53 Peptide, PDB code: 1ma3 was solved by J.L.Avalos, I.Celic, S.Muhammad, M.S.Cosgrove, J.D.Boeke, C.Wolberger, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	34.892, 35.591, 184.683, 90.00, 90.00, 90.00
R / Rfree (%)	20.9 / 25.4

The binding sites of Zinc atom in the Structure of A SIR2 Enzyme Bound to An Acetylated P53 Peptide (pdb code 1ma3). 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 Structure of A SIR2 Enzyme Bound to An Acetylated P53 Peptide, PDB code: 1ma3:

Zinc binding site 1 out of 1 in the Structure of A SIR2 Enzyme Bound to An Acetylated P53 Peptide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of A SIR2 Enzyme Bound to An Acetylated P53 Peptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1001 b:18.0 occ:1.00 SG A:CYS153 2.3 17.9 1.0 SG A:CYS126 2.4 15.2 1.0 SG A:CYS129 2.4 18.3 1.0 SG A:CYS150 2.5 17.4 1.0 CB A:CYS150 3.1 18.8 1.0 CB A:CYS129 3.2 17.6 1.0 CB A:CYS126 3.2 14.2 1.0 CB A:CYS153 3.4 16.6 1.0 N A:CYS129 3.7 18.5 1.0 N A:CYS153 3.8 19.1 1.0 CA A:CYS129 4.0 18.2 1.0 CA A:CYS153 4.1 17.3 1.0 CB A:SER155 4.4 14.4 1.0 CB A:LYS152 4.5 23.4 1.0 CA A:CYS150 4.6 19.2 1.0 C A:CYS129 4.6 18.1 1.0 CA A:CYS126 4.7 15.7 1.0 CB A:GLU131 4.8 20.3 1.0 C A:ASP128 4.8 19.7 1.0 C A:CYS153 4.8 17.2 1.0 N A:SER155 4.8 15.1 1.0 C A:LYS152 4.8 21.0 1.0 N A:HIS130 4.8 18.2 1.0 CB A:ASP128 4.8 23.4 1.0 N A:GLY154 4.9 17.8 1.0 N A:GLU131 5.0 18.9 1.0

J.L.Avalos, I.Celic, S.Muhammad, M.S.Cosgrove, J.D.Boeke, C.Wolberger. Structure of A SIR2 Enzyme Bound to An Acetylated P53 Peptide Mol.Cell V. 10 523 2002.
ISSN: ISSN 1097-2765
PubMed: 12408821
DOI: 10.1016/S1097-2765(02)00628-7