Atomistry » Chlorine » PDB 6f4l-6fbv » 6fav
Atomistry »
  Chlorine »
    PDB 6f4l-6fbv »
      6fav »

Chlorine in PDB 6fav: Crystal Structure of C-Terminal Modified Tau Peptide-Hybrid 4.2F-I with 14-3-3SIGMA

Protein crystallography data

The structure of Crystal Structure of C-Terminal Modified Tau Peptide-Hybrid 4.2F-I with 14-3-3SIGMA, PDB code: 6fav was solved by S.A.Andrei, F.A.Meijer, C.Ottmann, L.G.Milroy, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.33 / 1.40
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 62.789, 70.140, 128.259, 90.00, 90.00, 90.00
R / Rfree (%) 14.4 / 17.1

Other elements in 6fav:

The structure of Crystal Structure of C-Terminal Modified Tau Peptide-Hybrid 4.2F-I with 14-3-3SIGMA also contains other interesting chemical elements:

Sodium (Na) 5 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of C-Terminal Modified Tau Peptide-Hybrid 4.2F-I with 14-3-3SIGMA (pdb code 6fav). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of C-Terminal Modified Tau Peptide-Hybrid 4.2F-I with 14-3-3SIGMA, PDB code: 6fav:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 6fav

Go back to Chlorine Binding Sites List in 6fav
Chlorine binding site 1 out of 2 in the Crystal Structure of C-Terminal Modified Tau Peptide-Hybrid 4.2F-I with 14-3-3SIGMA


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of C-Terminal Modified Tau Peptide-Hybrid 4.2F-I with 14-3-3SIGMA within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl301

b:18.0
occ:1.00
O C:HOH682 3.0 33.0 1.0
HA C:TYR84 3.1 14.7 1.0
O C:HOH626 3.1 23.7 1.0
HD2 C:LYS87 3.2 27.7 1.0
HD1 C:TYR84 3.3 15.1 1.0
HB2 C:LYS87 3.4 19.4 1.0
HB3 C:GLU83 3.6 15.5 1.0
HD3 C:LYS87 3.8 27.7 1.0
HB2 C:TYR84 3.8 14.9 1.0
CA C:TYR84 3.9 12.2 1.0
CD C:LYS87 3.9 23.1 1.0
O C:GLU83 3.9 13.9 1.0
C C:GLU83 4.0 13.2 1.0
HB3 C:LYS87 4.0 19.4 1.0
N C:TYR84 4.0 11.9 1.0
CB C:LYS87 4.1 16.1 1.0
CD1 C:TYR84 4.2 12.6 1.0
CB C:TYR84 4.3 12.4 1.0
HB2 C:GLU83 4.3 15.5 1.0
CB C:GLU83 4.3 12.9 1.0
O C:HOH496 4.4 27.0 1.0
H C:TYR84 4.5 14.3 1.0
CG C:LYS87 4.6 19.2 1.0
HZ1 C:LYS87 4.7 39.9 1.0
HZ3 C:LYS87 4.7 39.9 1.0
CG C:TYR84 4.7 12.4 1.0
CA C:GLU83 4.8 13.4 1.0
HG3 C:LYS87 4.8 23.0 1.0
H C:LYS87 4.9 16.8 1.0
NZ C:LYS87 5.0 33.2 1.0

Chlorine binding site 2 out of 2 in 6fav

Go back to Chlorine Binding Sites List in 6fav
Chlorine binding site 2 out of 2 in the Crystal Structure of C-Terminal Modified Tau Peptide-Hybrid 4.2F-I with 14-3-3SIGMA


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of C-Terminal Modified Tau Peptide-Hybrid 4.2F-I with 14-3-3SIGMA within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl302

b:17.8
occ:1.00
HZ1 C:LYS9 2.2 18.0 1.0
HD3 C:LYS9 2.9 17.5 1.0
NZ C:LYS9 3.1 15.0 1.0
HZ3 C:LYS9 3.5 18.0 1.0
HZ C:PHE25 3.6 15.9 1.0
HZ2 C:LYS9 3.6 18.0 1.0
CD C:LYS9 3.7 14.6 1.0
HE2 C:LYS9 3.7 17.9 1.0
CE C:LYS9 3.7 14.9 1.0
HE2 C:MET1 3.8 18.6 1.0
HE1 C:PHE25 3.9 15.9 1.0
HD2 C:LYS9 4.1 17.5 1.0
O C:HOH660 4.1 48.7 1.0
CZ C:PHE25 4.3 13.3 1.0
HE3 C:MET1 4.3 18.6 1.0
CE1 C:PHE25 4.4 13.2 1.0
CE C:MET1 4.5 15.5 1.0
HE3 C:LYS9 4.6 17.9 1.0
HG2 C:LYS9 4.9 17.1 1.0
CG C:LYS9 4.9 14.3 1.0
O C:HOH687 4.9 44.3 1.0

Reference:

S.A.Andrei, F.A.Meijer, J.F.Neves, L.Brunsveld, I.Landrieu, C.Ottmann, L.G.Milroy. Inhibition of 14-3-3/Tau By Hybrid Small-Molecule Peptides Operating Via Two Different Binding Modes. Acs Chem Neurosci V. 9 2639 2018.
ISSN: ESSN 1948-7193
PubMed: 29722962
DOI: 10.1021/ACSCHEMNEURO.8B00118
Page generated: Sat Jul 12 13:58:20 2025

Last articles

Mg in 7FJP
Mg in 7FQJ
Mg in 7FGI
Mg in 7FGG
Mg in 7FJJ
Mg in 7FH8
Mg in 7FH9
Mg in 7FH7
Mg in 7FH6
Mg in 7FH4
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy