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

Protein crystallography data

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

Other elements in 5mxo:

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:

Chlorine (Cl) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium 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 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 Stabilized By Fusicoccin-A, PDB code: 5mxo:

Magnesium binding site 1 out of 1 in 5mxo

Go back to Magnesium Binding Sites List in 5mxo
Magnesium 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 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 Stabilized By Fusicoccin-A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg303

b:28.4
occ:1.00
O A:HOH575 2.2 42.1 1.0
O A:HOH600 2.3 43.9 1.0
O A:GLU161 2.3 24.3 1.0
O A:HOH537 2.5 42.1 1.0
C A:GLU161 3.5 20.1 1.0
HA A:MET162 3.5 24.4 0.4
HA A:MET162 3.6 22.9 0.6
HB3 A:GLU161 4.0 26.5 1.0
HA A:GLU161 4.1 22.5 1.0
HG3 A:MET162 4.2 28.4 0.4
HD3 A:PRO163 4.2 27.4 1.0
CA A:MET162 4.3 20.3 0.4
CA A:GLU161 4.4 18.8 1.0
N A:MET162 4.4 18.7 1.0
CA A:MET162 4.4 19.1 0.6
OE2 A:GLU115 4.5 35.2 0.6
CB A:GLU161 4.7 22.1 1.0
OE1 A:GLU161 4.7 37.9 1.0
HG2 A:MET162 4.9 22.4 0.6
HG2 A:MET162 5.0 28.4 0.4
CG A:MET162 5.0 23.7 0.4
CD A:PRO163 5.0 22.8 1.0
HD2 A:PRO163 5.0 27.4 1.0

Reference:

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
Page generated: Sun Sep 29 23:02:20 2024

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