Zinc in PDB 6rxj: Crystal Structure of Cobb Wt in Complex with H4K16-Acetyl Peptide

The structure of Crystal Structure of Cobb Wt in Complex with H4K16-Acetyl Peptide, PDB code: 6rxj 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)	46.38 / 1.60
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	131.100, 131.260, 58.540, 90.00, 90.00, 90.00
R / Rfree (%)	17.3 / 18.8

The binding sites of Zinc atom in the Crystal Structure of Cobb Wt in Complex with H4K16-Acetyl Peptide (pdb code 6rxj). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Cobb Wt in Complex with H4K16-Acetyl Peptide, PDB code: 6rxj:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Cobb Wt in Complex with H4K16-Acetyl 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-Acetyl Peptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:27.6 occ:0.82 SG A:CYS177 2.3 31.1 1.0 SG A:CYS174 2.3 32.1 1.0 SG A:CYS155 2.3 30.5 1.0 SG A:CYS176 2.4 34.1 1.0 HB2 A:CYS174 3.0 33.3 1.0 HB2 A:CYS177 3.0 45.8 1.0 CB A:CYS174 3.1 27.7 1.0 CB A:CYS177 3.2 38.2 1.0 HB3 A:CYS174 3.3 33.3 1.0 HB2 A:CYS155 3.3 41.0 1.0 H A:CYS176 3.3 39.3 1.0 H A:CYS177 3.4 32.4 1.0 CB A:CYS155 3.4 34.2 1.0 N A:CYS177 3.4 27.0 1.0 HB3 A:SER158 3.4 43.6 1.0 HG A:SER158 3.5 45.2 1.0 CB A:CYS176 3.7 42.7 1.0 HB3 A:CYS155 3.7 41.0 1.0 HB3 A:GLN157 3.7 52.3 1.0 OG A:SER158 3.7 37.7 1.0 C A:CYS176 3.7 33.0 1.0 H A:SER158 3.8 41.2 1.0 CA A:CYS177 3.9 32.7 1.0 HB3 A:ALA181 3.9 47.6 1.0 N A:CYS176 4.0 32.7 1.0 CA A:CYS176 4.0 39.4 1.0 HB3 A:CYS177 4.0 45.8 1.0 HB2 A:CYS176 4.0 51.2 1.0 H A:ALA181 4.1 41.5 1.0 CB A:SER158 4.1 36.3 1.0 HE21 A:GLN157 4.2 49.4 1.0 HA A:CYS177 4.3 39.3 1.0 O A:CYS176 4.4 35.7 1.0 HB3 A:CYS176 4.5 51.2 1.0 N A:SER158 4.5 34.4 1.0 CA A:CYS174 4.5 32.8 1.0 H A:GLN157 4.6 46.2 1.0 CB A:GLN157 4.7 43.6 1.0 CB A:ALA181 4.7 39.6 1.0 CA A:CYS155 4.7 34.2 1.0 HB2 A:ALA181 4.8 47.6 1.0 HB2 A:SER158 4.8 43.6 1.0 HA A:PRO180 4.8 42.6 1.0 N A:ALA181 4.8 34.6 1.0 HA A:CYS155 4.8 41.0 1.0 NE2 A:GLN157 4.8 41.1 1.0 HB2 A:GLN157 4.9 52.3 1.0 C A:CYS174 4.9 30.9 1.0 H A:HIS175 4.9 42.7 1.0 CA A:SER158 4.9 34.3 1.0 HA A:CYS176 4.9 47.3 1.0 N A:HIS175 5.0 35.6 1.0 H A:CYS174 5.0 36.7 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Cobb Wt in Complex with H4K16-Acetyl Peptide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Cobb Wt in Complex with H4K16-Acetyl Peptide within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn301 b:32.4 occ:1.00 O B:HOH520 1.9 55.8 1.0 SG B:CYS177 2.3 31.7 1.0 SG B:CYS174 2.3 31.3 1.0 SG B:CYS176 2.3 33.6 1.0 SG B:CYS155 2.4 30.3 1.0 HB2 B:CYS174 3.0 32.3 1.0 HB2 B:CYS177 3.0 42.1 1.0 CB B:CYS174 3.1 26.9 1.0 CB B:CYS177 3.2 35.1 1.0 HB2 B:CYS155 3.3 36.0 1.0 HB3 B:CYS174 3.3 32.3 1.0 H B:CYS176 3.3 36.7 1.0 H B:CYS177 3.3 35.2 1.0 N B:CYS177 3.4 29.3 1.0 CB B:CYS155 3.4 30.0 1.0 HB3 B:SER158 3.5 43.2 1.0 HG B:SER158 3.5 44.1 1.0 CB B:CYS176 3.6 38.7 1.0 HB3 B:CYS155 3.7 36.0 1.0 C B:CYS176 3.7 32.8 1.0 OG B:SER158 3.8 36.8 1.0 H B:SER158 3.8 43.4 1.0 CA B:CYS177 3.9 31.1 1.0 N B:CYS176 3.9 30.6 1.0 HB2 B:CYS176 4.0 46.5 1.0 CA B:CYS176 4.0 35.4 1.0 HB2 B:GLN157 4.0 55.1 1.0 HB3 B:ALA181 4.0 44.8 1.0 HB3 B:CYS177 4.0 42.1 1.0 H B:ALA181 4.0 40.9 1.0 CB B:SER158 4.1 36.0 1.0 HA B:CYS177 4.3 37.3 1.0 HB3 B:CYS176 4.4 46.5 1.0 O B:CYS176 4.4 34.9 1.0 CA B:CYS174 4.5 36.0 1.0 N B:SER158 4.5 36.2 1.0 H B:GLN157 4.6 48.5 1.0 CA B:CYS155 4.7 31.5 1.0 HA B:PRO180 4.8 45.3 1.0 HA B:CYS155 4.8 37.8 1.0 N B:ALA181 4.8 34.1 1.0 CB B:ALA181 4.8 37.3 1.0 HB2 B:SER158 4.8 43.2 1.0 HB2 B:ALA181 4.9 44.8 1.0 CB B:GLN157 4.9 45.9 1.0 C B:CYS174 4.9 31.7 1.0 HA B:CYS176 4.9 42.5 1.0 H B:HIS175 4.9 44.5 1.0 H B:CYS174 5.0 39.2 1.0 N B:HIS175 5.0 37.1 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