Zinc in PDB 1s5p: Structure and Substrate Binding Properties of Cobb, A SIR2 Homolog Protein Deacetylase From Eschericia Coli.

The structure of Structure and Substrate Binding Properties of Cobb, A SIR2 Homolog Protein Deacetylase From Eschericia Coli., PDB code: 1s5p was solved by K.Zhao, X.Chai, R.Marmorstein, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.70 / 1.96
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	93.911, 93.911, 61.488, 90.00, 90.00, 90.00
R / Rfree (%)	23.4 / 27

The binding sites of Zinc atom in the Structure and Substrate Binding Properties of Cobb, A SIR2 Homolog Protein Deacetylase From Eschericia Coli. (pdb code 1s5p). 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 and Substrate Binding Properties of Cobb, A SIR2 Homolog Protein Deacetylase From Eschericia Coli., PDB code: 1s5p:

Zinc binding site 1 out of 1 in the Structure and Substrate Binding Properties of Cobb, A SIR2 Homolog Protein Deacetylase From Eschericia Coli.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure and Substrate Binding Properties of Cobb, A SIR2 Homolog Protein Deacetylase From Eschericia Coli. within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1001 b:0.8 occ:1.00 CB A:CYS174 2.3 85.8 1.0 SG A:CYS174 2.6 84.4 1.0 SG A:CYS155 2.9 0.8 1.0 CB A:CYS155 3.1 90.1 1.0 CA A:CYS174 3.5 86.8 1.0 N A:SER158 3.9 87.6 1.0 CB A:SER158 3.9 88.0 1.0 N A:CYS174 4.0 88.3 1.0 CB A:GLN157 4.1 97.2 1.0 CA A:CYS155 4.6 83.7 1.0 CA A:SER158 4.6 87.3 1.0 N A:GLN157 4.7 90.8 1.0 CA A:GLN157 4.7 92.4 1.0 C A:GLN157 4.7 89.6 1.0 C A:CYS174 4.8 85.6 1.0 CG A:GLN157 4.9 99.5 1.0 C A:CYS155 4.9 84.9 1.0 O A:PRO182 4.9 72.5 1.0

K.Zhao, X.Chai, R.Marmorstein. Structure and Substrate Binding Properties of Cobb, A SIR2 Homolog Protein Deacetylase From Eschericia Coli. J.Mol.Biol. V. 337 731 2004.
ISSN: ISSN 0022-2836
PubMed: 15019790
DOI: 10.1016/J.JMB.2004.01.060