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Zinc in PDB 6rxl: Crystal Structure of Cobb Wt in Complex with H4K16-Crotonyl Peptide

Protein crystallography data

The structure of Crystal Structure of Cobb Wt in Complex with H4K16-Crotonyl Peptide, PDB code: 6rxl 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) 46.98 / 2.30
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 93.960, 93.960, 58.540, 90.00, 90.00, 90.00
R / Rfree (%) 21.2 / 25

Zinc Binding Sites:

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

Zinc binding site 1 out of 1 in 6rxl

Go back to Zinc Binding Sites List in 6rxl
Zinc binding site 1 out of 1 in the Crystal Structure of Cobb Wt in Complex with H4K16-Crotonyl 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-Crotonyl Peptide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:85.9
occ:1.00
SG A:CYS174 2.4 92.6 1.0
SG A:CYS176 2.4 88.0 1.0
SG A:CYS155 2.5 89.5 1.0
SG A:CYS177 2.5 91.2 1.0
CB A:CYS174 3.0 93.8 1.0
CB A:SER158 3.4 79.4 1.0
CB A:CYS177 3.4 94.8 1.0
CB A:CYS155 3.4 74.9 1.0
N A:CYS177 3.5 92.6 1.0
CB A:CYS176 3.9 93.9 1.0
CA A:CYS177 4.0 96.1 1.0
C A:CYS176 4.1 93.8 1.0
OG A:SER158 4.2 79.5 1.0
N A:CYS176 4.2 94.4 1.0
CA A:CYS176 4.3 97.7 1.0
CA A:CYS174 4.4 91.5 1.0
N A:SER158 4.5 77.0 1.0
CA A:SER158 4.5 79.6 1.0
CB A:ALA181 4.6 89.2 1.0
CG A:GLN157 4.7 93.0 1.0
C A:CYS174 4.8 92.3 1.0
CA A:CYS155 4.8 67.5 1.0
N A:ALA181 4.9 93.7 1.0

Reference:

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
Page generated: Thu Aug 21 19:21:24 2025

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