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

Protein crystallography data

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

Zinc Binding Sites:

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 6rxk

Go back to Zinc Binding Sites List in 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

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: Wed Dec 16 12:43:39 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy