Zinc in PDB 6rxk: Crystal Structure of Cobb Wt in Complex with H4K16-Butyryl Peptide

The structure of Crystal Structure of Cobb Wt in Complex with H4K16-Butyryl Peptide, PDB code: 6rxk was solved by M.Spinck, R.Gasper, H.Neumann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.37 / 1.35
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	92.730, 92.730, 58.620, 90.00, 90.00, 90.00
R / Rfree (%)	17 / 18.8

The binding sites of Zinc atom in the Crystal Structure of Cobb Wt in Complex with H4K16-Butyryl Peptide (pdb code 6rxk). 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 Crystal Structure of Cobb Wt in Complex with H4K16-Butyryl Peptide, PDB code: 6rxk:

Zinc binding site 1 out of 1 in the Crystal Structure of Cobb Wt in Complex with H4K16-Butyryl Peptide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Cobb Wt in Complex with H4K16-Butyryl Peptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:19.9 occ:1.00 SG A:CYS177 2.2 20.5 1.0 SG A:CYS155 2.3 19.5 1.0 SG A:CYS174 2.3 19.0 1.0 SG A:CYS176 2.4 20.8 1.0 HB2 A:CYS174 2.9 21.5 1.0 CB A:CYS174 3.1 17.9 1.0 HB2 A:CYS177 3.1 20.7 1.0 HB3 A:CYS174 3.2 21.5 1.0 CB A:CYS177 3.2 17.2 1.0 HB2 A:CYS155 3.3 18.4 1.0 H A:CYS177 3.3 22.4 1.0 H A:CYS176 3.3 22.1 1.0 HB3 A:SER158 3.3 25.3 1.0 N A:CYS177 3.4 18.7 1.0 CB A:CYS155 3.4 15.4 1.0 HG A:SER158 3.6 26.4 1.0 H A:SER158 3.6 28.5 1.0 HB3 A:ALA181 3.6 27.4 1.0 CB A:CYS176 3.7 21.8 1.0 C A:CYS176 3.7 20.4 1.0 HB3 A:CYS155 3.7 18.4 1.0 OG A:SER158 3.7 22.0 1.0 HB3 A:GLN157 3.7 31.0 1.0 CA A:CYS177 3.9 21.6 1.0 CA A:CYS176 3.9 20.9 1.0 N A:CYS176 3.9 18.5 1.0 HB2 A:CYS176 3.9 26.1 1.0 CB A:SER158 4.0 21.1 1.0 HB3 A:CYS177 4.1 20.7 1.0 H A:ALA181 4.1 25.9 1.0 HA A:CYS177 4.3 25.9 1.0 N A:SER158 4.3 23.7 1.0 O A:CYS176 4.4 23.2 1.0 HB3 A:CYS176 4.4 26.1 1.0 HB2 A:ALA181 4.5 27.4 1.0 CB A:ALA181 4.5 22.9 1.0 CA A:CYS174 4.5 20.4 1.0 H A:GLN157 4.5 29.1 1.0 HA A:PRO180 4.7 24.1 1.0 CB A:GLN157 4.7 25.8 1.0 CA A:CYS155 4.7 19.0 1.0 HB2 A:SER158 4.7 25.3 1.0 N A:ALA181 4.8 21.6 1.0 HA A:CYS155 4.8 22.8 1.0 CA A:SER158 4.8 22.6 1.0 O A:HOH684 4.9 30.9 1.0 C A:CYS174 4.9 19.8 1.0 HA A:CYS176 4.9 25.0 1.0 HG2 A:GLN157 5.0 53.3 1.0 H A:CYS174 5.0 25.3 1.0 OE1 A:GLN157 5.0 29.2 1.0

M.Spinck, P.Neumann-Staubitz, M.Ecke, R.Gasper, H.Neumann. Evolved, Selective Erasers of Distinct Lysine Acylations. Angew.Chem.Int.Ed.Engl. 2020.
ISSN: ESSN 1521-3773
PubMed: 32187803
DOI: 10.1002/ANIE.202002899