Magnesium in PDB 5moc: Crystal Structure of 14-3-3SIGMA and A P53 C-Terminal 12-Mer Synthetic Phosphopeptide

The structure of Crystal Structure of 14-3-3SIGMA and A P53 C-Terminal 12-Mer Synthetic Phosphopeptide, PDB code: 5moc 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)	25.60 / 1.80
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	81.910, 112.270, 62.420, 90.00, 90.00, 90.00
R / Rfree (%)	16.5 / 20.8

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

Chlorine

(Cl)

1 atom

The binding sites of Magnesium atom in the Crystal Structure of 14-3-3SIGMA and A P53 C-Terminal 12-Mer Synthetic Phosphopeptide (pdb code 5moc). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of 14-3-3SIGMA and A P53 C-Terminal 12-Mer Synthetic Phosphopeptide, PDB code: 5moc:

Magnesium binding site 1 out of 1 in the Crystal Structure of 14-3-3SIGMA and A P53 C-Terminal 12-Mer Synthetic Phosphopeptide


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of 14-3-3SIGMA and A P53 C-Terminal 12-Mer Synthetic Phosphopeptide within 5.0Å range: probe atom residue distance (Å) B Occ P:Mg401 b:14.6 occ:0.61 O P:HOH503 2.1 24.1 1.0 OD2 P:ASP391 2.1 46.7 1.0 O P:HOH505 2.2 29.2 1.0 O P:HOH519 2.3 32.4 1.0 OD2 P:ASP393 2.4 30.9 1.0 O P:HOH522 2.5 36.2 1.0 CG P:ASP391 3.3 47.7 1.0 CG P:ASP393 3.3 30.8 1.0 HA P:ASP391 3.6 54.0 1.0 OD1 P:ASP393 3.7 28.9 1.0 HB3 P:MET384 3.7 28.3 1.0 O P:HOH521 3.7 27.5 1.0 H P:ASP393 3.8 58.3 1.0 HB2 P:MET384 3.9 28.3 1.0 OD1 P:ASP391 4.0 48.0 1.0 HG3 P:MET384 4.1 30.4 1.0 CB P:MET384 4.2 23.6 1.0 CA P:ASP391 4.3 45.0 1.0 OXT P:ASP393 4.4 58.9 1.0 CB P:ASP391 4.4 48.0 1.0 O P:HOH507 4.4 15.5 1.0 O P:HOH509 4.4 45.4 1.0 O P:HOH516 4.5 27.9 1.0 C P:ASP393 4.5 53.5 1.0 O1P P:TPO387 4.5 18.2 1.0 N P:ASP393 4.6 48.6 1.0 CB P:ASP393 4.6 35.0 1.0 C P:ASP391 4.6 46.3 1.0 CG P:MET384 4.7 25.3 1.0 O P:PHE385 4.7 19.5 1.0 HB2 P:ASP391 4.8 57.6 1.0 CA P:ASP393 4.8 45.8 1.0 HE2 P:MET384 4.8 31.0 1.0 H P:SER392 4.8 57.5 1.0 HE3 P:MET384 4.9 31.0 1.0 O P:ASP393 4.9 54.5 1.0 HH22 A:ARG60 5.0 22.6 1.0 N P:SER392 5.0 47.9 1.0 HH12 A:ARG56 5.0 15.4 1.0

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