Chlorine in PDB 7obt: Crystal Structure of 14-3-3 Sigma in Complex with RIPK2 Phosphopeptide and Stabilizer Fusicoccin-A

Enzymatic activity of Crystal Structure of 14-3-3 Sigma in Complex with RIPK2 Phosphopeptide and Stabilizer Fusicoccin-A

All present enzymatic activity of Crystal Structure of 14-3-3 Sigma in Complex with RIPK2 Phosphopeptide and Stabilizer Fusicoccin-A:
2.7.10.2; 2.7.11.1;

Protein crystallography data

The structure of Crystal Structure of 14-3-3 Sigma in Complex with RIPK2 Phosphopeptide and Stabilizer Fusicoccin-A, PDB code: 7obt was solved by F.Centorrino, B.Andlovic, C.Ottmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 31.34 / 2.30
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 82.952, 111.88, 62.686, 90, 90, 90
R / Rfree (%) 20.4 / 24.6

Other elements in 7obt:

The structure of Crystal Structure of 14-3-3 Sigma in Complex with RIPK2 Phosphopeptide and Stabilizer Fusicoccin-A also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of 14-3-3 Sigma in Complex with RIPK2 Phosphopeptide and Stabilizer Fusicoccin-A (pdb code 7obt). 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 Crystal Structure of 14-3-3 Sigma in Complex with RIPK2 Phosphopeptide and Stabilizer Fusicoccin-A, PDB code: 7obt:

Chlorine binding site 1 out of 1 in 7obt

Go back to Chlorine Binding Sites List in 7obt
Chlorine binding site 1 out of 1 in the Crystal Structure of 14-3-3 Sigma in Complex with RIPK2 Phosphopeptide and Stabilizer Fusicoccin-A


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 14-3-3 Sigma in Complex with RIPK2 Phosphopeptide and Stabilizer Fusicoccin-A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl404

b:16.9
occ:1.00
 HZ3 A:LYS9 2.3 13.6 1.0
HD3 A:LYS9 3.0 12.0 1.0
NZ A:LYS9 3.1 11.3 1.0
HZ2 A:LYS9 3.3 13.6 1.0
HZ A:PHE25 3.6 12.8 1.0
CD A:LYS9 3.7 10.0 1.0
HZ1 A:LYS9 3.7 13.6 1.0
HE1 A:MET1 3.9 13.0 1.0
CE A:LYS9 3.9 11.2 1.0
HD2 A:LYS9 3.9 12.0 1.0
HE1 A:PHE25 4.0 8.1 1.0
HE2 A:LYS9 4.1 13.5 1.0
CZ A:PHE25 4.3 10.6 1.0
HE2 A:MET1 4.5 13.0 1.0
CE1 A:PHE25 4.5 6.8 1.0
CE A:MET1 4.6 10.8 1.0
HE3 A:LYS9 4.8 13.5 1.0
O A:HOH669 4.9 28.4 1.0

Reference:

B.Andlovic, G.Heilmann, S.Ninck, S.Andrei, F.Centorrino, Y.Higuchi, N.Kato, L.Brunsveld, S.Menninger, A.Choidas, A.Wolf, M.Kaiser, J.Eickhoff, C.Ottmann. Inf Alpha Primes Ovarian Cancer Cells For Fusicoccin-Induced Cell Death Via Stabilization of 14-3-3 Protein-Protein Interactions To Be Published.
Page generated: Tue Jul 30 01:26:04 2024

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