Zinc in PDB 6rxo: Crystal Structure of Cobb AC2 (A76G, I131C, V162A) in Complex with H4K16-Buturyl Peptide

The structure of Crystal Structure of Cobb AC2 (A76G, I131C, V162A) in Complex with H4K16-Buturyl Peptide, PDB code: 6rxo 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)	47.23 / 1.95
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	60.490, 92.440, 94.450, 90.00, 90.00, 90.00
R / Rfree (%)	19.7 / 21.5

The binding sites of Zinc atom in the Crystal Structure of Cobb AC2 (A76G, I131C, V162A) in Complex with H4K16-Buturyl Peptide (pdb code 6rxo). 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 AC2 (A76G, I131C, V162A) in Complex with H4K16-Buturyl Peptide, PDB code: 6rxo:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Cobb AC2 (A76G, I131C, V162A) in Complex with H4K16-Buturyl 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 AC2 (A76G, I131C, V162A) in Complex with H4K16-Buturyl Peptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:48.5 occ:1.00 SG A:CYS174 2.3 47.7 1.0 SG A:CYS177 2.4 44.9 1.0 SG A:CYS155 2.4 46.6 1.0 SG A:CYS176 2.4 48.4 1.0 CB A:CYS174 3.0 46.5 1.0 CB A:CYS177 3.1 48.0 1.0 N A:CYS177 3.3 54.2 1.0 CB A:CYS155 3.4 47.0 1.0 C A:CYS176 3.7 54.7 1.0 CB A:CYS176 3.7 53.0 1.0 CA A:CYS177 3.7 54.2 1.0 OG A:SER158 3.8 55.2 1.0 N A:CYS176 3.9 51.2 1.0 CA A:CYS176 3.9 54.0 1.0 CB A:SER158 4.2 52.7 1.0 O A:CYS176 4.4 51.2 1.0 CA A:CYS174 4.5 42.8 1.0 N A:SER158 4.5 50.0 1.0 CB A:ALA181 4.6 46.9 1.0 CA A:CYS155 4.7 45.4 1.0 C A:CYS174 4.8 54.4 1.0 N A:ALA181 4.8 53.5 1.0 CB A:GLN157 4.8 52.0 1.0 N A:HIS175 4.8 52.2 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Cobb AC2 (A76G, I131C, V162A) in Complex with H4K16-Buturyl 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 AC2 (A76G, I131C, V162A) in Complex with H4K16-Buturyl Peptide within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn301 b:70.4 occ:1.00 SG B:CYS176 2.4 73.6 1.0 SG B:CYS174 2.4 80.6 1.0 SG B:CYS155 2.4 70.8 1.0 SG B:CYS177 2.5 71.5 1.0 CB B:CYS174 3.2 73.5 1.0 CB B:CYS155 3.2 66.2 1.0 CB B:CYS177 3.3 73.5 1.0 OG B:SER158 3.4 71.1 1.0 N B:CYS177 3.4 83.7 1.0 CB B:CYS176 3.8 84.5 1.0 C B:CYS176 3.8 85.3 1.0 CB B:SER158 3.8 69.5 1.0 CA B:CYS177 3.9 85.7 1.0 N B:CYS176 4.0 80.9 1.0 CA B:CYS176 4.1 85.2 1.0 O B:CYS176 4.4 82.4 1.0 CB B:ALA181 4.4 71.3 1.0 N B:SER158 4.5 67.2 1.0 CA B:CYS174 4.6 73.9 1.0 CA B:CYS155 4.6 58.2 1.0 N B:ALA181 4.7 77.9 1.0 CA B:SER158 4.8 64.9 1.0 C B:CYS174 4.9 84.1 1.0 N B:HIS175 5.0 80.5 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