Zinc in PDB 4kxq: Structure of Nad-Dependent Protein Deacetylase Sirtuin-1 (Closed State, 1.85 A)

The structure of Structure of Nad-Dependent Protein Deacetylase Sirtuin-1 (Closed State, 1.85 A), PDB code: 4kxq was solved by A.M.Davenport, F.M.Huber, A.Hoelz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.36 / 1.85
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	92.714, 92.714, 97.745, 90.00, 90.00, 120.00
R / Rfree (%)	16.8 / 18.9

The binding sites of Zinc atom in the Structure of Nad-Dependent Protein Deacetylase Sirtuin-1 (Closed State, 1.85 A) (pdb code 4kxq). 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 Nad-Dependent Protein Deacetylase Sirtuin-1 (Closed State, 1.85 A), PDB code: 4kxq:

Zinc binding site 1 out of 1 in the Structure of Nad-Dependent Protein Deacetylase Sirtuin-1 (Closed State, 1.85 A)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Nad-Dependent Protein Deacetylase Sirtuin-1 (Closed State, 1.85 A) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn601 b:49.3 occ:1.00 SG A:CYS398 2.3 47.5 1.0 SG A:CYS371 2.3 37.5 1.0 SG A:CYS395 2.4 45.0 1.0 SG A:CYS374 2.4 37.8 1.0 HB3 A:CYS374 3.0 48.1 1.0 HB2 A:CYS398 3.1 67.1 1.0 HB2 A:CYS395 3.1 55.6 1.0 HB3 A:CYS371 3.1 45.5 1.0 CB A:CYS395 3.1 46.3 1.0 CB A:CYS371 3.2 37.9 1.0 HB2 A:CYS371 3.2 45.5 1.0 H A:CYS374 3.2 45.6 1.0 H A:CYS398 3.2 71.1 1.0 HB3 A:CYS395 3.2 55.6 1.0 CB A:CYS374 3.3 40.1 1.0 CB A:CYS398 3.3 56.0 1.0 HB1 A:ALA405 3.6 62.8 1.0 HB A:ILE373 3.7 51.0 1.0 N A:CYS374 3.8 38.0 1.0 N A:CYS398 3.8 59.3 1.0 HB3 A:ARG397 3.8 72.5 1.0 HB3 A:TYR376 3.9 55.3 1.0 HE A:ARG397 4.0 75.6 1.0 HB2 A:CYS374 4.0 48.1 1.0 HB3 A:CYS398 4.1 67.1 1.0 CA A:CYS398 4.1 61.2 1.0 CA A:CYS374 4.1 38.7 1.0 H A:TYR376 4.2 47.4 1.0 HA A:CYS398 4.4 73.5 1.0 H A:ILE373 4.4 47.7 1.0 CB A:ALA405 4.4 52.3 1.0 HA A:ALA405 4.4 61.7 1.0 HB2 A:ALA405 4.4 62.8 1.0 HB2 A:TYR376 4.4 55.3 1.0 H A:ARG397 4.5 74.5 1.0 H A:LYS375 4.6 44.4 1.0 CB A:TYR376 4.6 46.0 1.0 CA A:CYS395 4.6 48.9 1.0 CB A:ILE373 4.6 42.5 1.0 CA A:CYS371 4.6 36.6 1.0 HG22 A:ILE373 4.7 52.1 1.0 HH21 A:ARG397 4.7 71.7 1.0 HG2 A:ARG397 4.7 97.0 1.0 CB A:ARG397 4.7 60.5 1.0 C A:CYS374 4.8 38.9 1.0 C A:ARG397 4.8 64.9 1.0 C A:ILE373 4.8 39.2 1.0 HA A:CYS395 4.9 58.7 1.0 NE A:ARG397 4.9 63.0 1.0 N A:LYS375 4.9 37.0 1.0 CA A:ALA405 4.9 51.4 1.0 HA A:CYS374 4.9 46.4 1.0 HA A:CYS371 5.0 43.9 1.0

A.M.Davenport, F.M.Huber, A.Hoelz. Structural and Functional Analysis of Human SIRT1. J.Mol.Biol. V. 426 526 2014.
ISSN: ISSN 0022-2836
PubMed: 24120939
DOI: 10.1016/J.JMB.2013.10.009