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Chlorine in PDB 7bgq: 14-3-3 Sigma with PIN1 Binding Site PS72 and Covalently Bound LVD1019
Enzymatic activity of 14-3-3 Sigma with PIN1 Binding Site PS72 and Covalently Bound LVD1019
All present enzymatic activity of 14-3-3 Sigma with PIN1 Binding Site PS72 and Covalently Bound LVD1019:
5.2.1.8;
5.2.1.8;
Protein crystallography data
The structure of 14-3-3 Sigma with PIN1 Binding Site PS72 and Covalently Bound LVD1019, PDB code: 7bgq
was solved by
M.Wolter,
L.V.Dijck,
P.J.Cossar,
C.Ottmann,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
| Resolution Low / High (Å) | 33.98 / 1.75 |
| Space group | C 2 2 21 |
| Cell size a, b, c (Å), α, β, γ (°) | 82.3, 111.928, 62.427, 90, 90, 90 |
| R / Rfree (%) | 17.1 / 20.8 |
Other elements in 7bgq:
The structure of 14-3-3 Sigma with PIN1 Binding Site PS72 and Covalently Bound LVD1019 also contains other interesting chemical elements:
| Calcium | (Ca) | 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 LVD1019
(pdb code 7bgq). 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 LVD1019, PDB code: 7bgq:
In total only one binding site of Chlorine was determined in the 14-3-3 Sigma with PIN1 Binding Site PS72 and Covalently Bound LVD1019, PDB code: 7bgq:
Chlorine binding site 1 out of 1 in 7bgq
Go back to
Chlorine Binding Sites List in 7bgq
Chlorine binding site 1 out
of 1 in the 14-3-3 Sigma with PIN1 Binding Site PS72 and Covalently Bound LVD1019
Mono view
Stereo pair view
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 LVD1019 within 5.0Å range:
|
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 23:17:12 2025
ISSN: ESSN 1520-5126
PubMed: 34047554
DOI: 10.1021/JACS.1C03035
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