Chlorine in PDB 5mxo: Crystal Structure of 14-3-3SIGMA and A P53 C-Terminal 12-Mer Synthetic Phosphopeptide Stabilized By Fusicoccin-A

The structure of Crystal Structure of 14-3-3SIGMA and A P53 C-Terminal 12-Mer Synthetic Phosphopeptide Stabilized By Fusicoccin-A, PDB code: 5mxo was solved by S.Andrei, C.Ottmann, S.Leysen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.59 / 1.20
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	82.688, 111.560, 62.690, 90.00, 90.00, 90.00
R / Rfree (%)	15.4 / 18.2

The structure of Crystal Structure of 14-3-3SIGMA and A P53 C-Terminal 12-Mer Synthetic Phosphopeptide Stabilized By Fusicoccin-A also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Chlorine atom in the Crystal Structure of 14-3-3SIGMA and A P53 C-Terminal 12-Mer Synthetic Phosphopeptide Stabilized By Fusicoccin-A (pdb code 5mxo). 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 14-3-3SIGMA and A P53 C-Terminal 12-Mer Synthetic Phosphopeptide Stabilized By Fusicoccin-A, PDB code: 5mxo:

Chlorine binding site 1 out of 1 in the Crystal Structure of 14-3-3SIGMA and A P53 C-Terminal 12-Mer Synthetic Phosphopeptide Stabilized By 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 14-3-3SIGMA and A P53 C-Terminal 12-Mer Synthetic Phosphopeptide Stabilized By Fusicoccin-A within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl302 b:17.3 occ:0.98 O A:HOH662 3.0 28.6 1.0 HA A:TYR84 3.0 15.2 1.0 O A:HOH627 3.1 24.6 1.0 HD2 A:LYS87 3.1 25.2 0.3 HD2 A:LYS87 3.1 30.0 0.7 HD1 A:TYR84 3.3 17.2 1.0 HB2 A:LYS87 3.4 20.1 0.3 HB2 A:LYS87 3.4 20.6 0.7 HB3 A:GLU83 3.6 16.9 1.0 HB2 A:TYR84 3.7 16.0 1.0 HD3 A:LYS87 3.8 30.0 0.7 CA A:TYR84 3.8 12.7 1.0 CD A:LYS87 3.9 25.0 0.7 O A:GLU83 3.9 14.5 1.0 CD A:LYS87 4.0 21.0 0.3 N A:TYR84 4.0 13.4 1.0 HB3 A:LYS87 4.0 20.1 0.3 HB3 A:LYS87 4.0 20.6 0.7 C A:GLU83 4.0 13.8 1.0 CD1 A:TYR84 4.0 14.3 1.0 HD3 A:LYS87 4.1 25.2 0.3 CB A:LYS87 4.1 17.2 0.7 CB A:LYS87 4.1 16.7 0.3 CB A:TYR84 4.2 13.3 1.0 HB2 A:GLU83 4.3 16.9 1.0 CB A:GLU83 4.3 14.1 1.0 H A:TYR84 4.4 16.1 1.0 CG A:LYS87 4.5 21.1 0.7 O A:HOH462 4.5 23.4 1.0 CG A:TYR84 4.6 13.1 1.0 CG A:LYS87 4.6 18.4 0.3 HZ3 A:LYS87 4.7 38.7 0.7 HG3 A:LYS87 4.8 25.3 0.7 O A:HOH672 4.8 47.9 1.0 HG3 A:LYS87 4.8 22.1 0.3 CA A:GLU83 4.8 13.5 1.0 HZ2 A:LYS87 4.8 38.7 0.7 H A:LYS87 4.8 20.3 0.3 HZ2 A:LYS87 5.0 30.2 0.3 H A:LYS87 5.0 18.1 0.7

R.G.Doveston, A.Kuusk, S.A.Andrei, S.Leysen, Q.Cao, M.P.Castaldi, A.Hendricks, L.Brunsveld, H.Chen, H.Boyd, C.Ottmann. Small-Molecule Stabilization of the P53 - 14-3-3 Protein-Protein Interaction. Febs Lett. V. 591 2449 2017.
ISSN: ISSN 1873-3468
PubMed: 28640363
DOI: 10.1002/1873-3468.12723