Chlorine in PDB 6yp3: 14-3-3 Sigma with Rela/P65 Binding Site PS45 and Covalently Bound TCF521-028

Protein crystallography data

The structure of 14-3-3 Sigma with Rela/P65 Binding Site PS45 and Covalently Bound TCF521-028, PDB code: 6yp3 was solved by M.Wolter, C.Ottmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 41.77 / 1.80
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 82.498, 112.220, 62.550, 90.00, 90.00, 90.00
R / Rfree (%) 18.1 / 21.5

Chlorine Binding Sites:

The binding sites of Chlorine atom in the 14-3-3 Sigma with Rela/P65 Binding Site PS45 and Covalently Bound TCF521-028 (pdb code 6yp3). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the 14-3-3 Sigma with Rela/P65 Binding Site PS45 and Covalently Bound TCF521-028, PDB code: 6yp3:

Chlorine binding site 1 out of 1 in 6yp3

Go back to Chlorine Binding Sites List in 6yp3
Chlorine binding site 1 out of 1 in the 14-3-3 Sigma with Rela/P65 Binding Site PS45 and Covalently Bound TCF521-028


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of 14-3-3 Sigma with Rela/P65 Binding Site PS45 and Covalently Bound TCF521-028 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl301

b:19.5
occ:1.00
O A:HOH682 2.9 22.4 1.0
O A:HOH667 3.0 22.6 1.0
CA A:TYR84 3.8 11.0 1.0
CD A:LYS87 3.8 21.1 1.0
O A:GLU83 3.9 7.4 1.0
CD1 A:TYR84 4.0 6.1 1.0
N A:TYR84 4.1 5.7 1.0
CB A:LYS87 4.1 13.4 1.0
C A:GLU83 4.1 9.1 1.0
CB A:TYR84 4.3 6.2 1.0
CB A:GLU83 4.5 7.6 1.0
O A:HOH458 4.5 16.1 1.0
CG A:LYS87 4.5 17.5 1.0
CG A:TYR84 4.6 7.2 1.0
CA A:GLU83 4.9 6.5 1.0

Reference:

M.Wolter, D.Valenti, P.J.Cossar, L.M.Levy, S.Hristeva, T.Genski, T.Hoffmann, L.Brunsveld, D.Tzalis, C.Ottmann. Fragment-Based Stabilizers of Protein-Protein Interactions Through Imine-Based Tethering. Angew.Chem.Int.Ed.Engl. 2020.
ISSN: ESSN 1521-3773
PubMed: 32816380
DOI: 10.1002/ANIE.202008585
Page generated: Sat Dec 12 14:43:40 2020

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