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Chlorine in PDB 7az2: 14-3-3 Sigma with PIN1 Binding Site PS72 and Covalently Bound LVD1014

Enzymatic activity of 14-3-3 Sigma with PIN1 Binding Site PS72 and Covalently Bound LVD1014

All present enzymatic activity of 14-3-3 Sigma with PIN1 Binding Site PS72 and Covalently Bound LVD1014:
5.2.1.8;

Protein crystallography data

The structure of 14-3-3 Sigma with PIN1 Binding Site PS72 and Covalently Bound LVD1014, PDB code: 7az2 was solved by M.Wolter, L.V.Dijck, C.Ottmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 66.24 / 1.08
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 82.142, 112.024, 62.456, 90, 90, 90
R / Rfree (%) 18.5 / 19.7

Other elements in 7az2:

The structure of 14-3-3 Sigma with PIN1 Binding Site PS72 and Covalently Bound LVD1014 also contains other interesting chemical elements:

Calcium (Ca) 2 atoms
Fluorine (F) 3 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the 14-3-3 Sigma with PIN1 Binding Site PS72 and Covalently Bound LVD1014 (pdb code 7az2). 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 PIN1 Binding Site PS72 and Covalently Bound LVD1014, PDB code: 7az2:

Chlorine binding site 1 out of 1 in 7az2

Go back to Chlorine Binding Sites List in 7az2
Chlorine binding site 1 out of 1 in the 14-3-3 Sigma with PIN1 Binding Site PS72 and Covalently Bound LVD1014


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 PIN1 Binding Site PS72 and Covalently Bound LVD1014 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl304

b:24.4
occ:1.00
NZ A:LYS9 3.1 18.9 1.0
CE A:LYS9 3.7 16.1 1.0
CD A:LYS9 3.7 15.6 1.0
CZ A:PHE25 4.3 13.3 1.0
CE2 A:PHE25 4.5 13.8 1.0
CE A:MET1 4.7 18.4 1.0
CG A:LYS9 4.9 13.3 1.0

Reference:

P.J.Cossar, M.Wolter, L.Van Dijck, D.Valenti, L.M.Levy, C.Ottmann, L.Brunsveld. Reversible Covalent Imine-Tethering For Selective Stabilization of 14-3-3 Hub Protein Interactions. J.Am.Chem.Soc. 2021.
ISSN: ESSN 1520-5126
PubMed: 34047554
DOI: 10.1021/JACS.1C03035
Page generated: Sat Jul 12 23:01:36 2025

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