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

Protein crystallography data

The structure of Crystal Structure of 14-3-3SIGMA and A P53 C-Terminal 12-Mer Synthetic Phosphopeptide, PDB code: 5mhc 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) 45.44 / 1.20
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 82.114, 112.047, 62.470, 90.00, 90.00, 90.00
R / Rfree (%) 15 / 16.5

Other elements in 5mhc:

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

Calcium (Ca) 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 (pdb code 5mhc). 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: 5mhc:

Magnesium binding site 1 out of 1 in 5mhc

Go back to Magnesium Binding Sites List in 5mhc
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
A:Mg302

b:24.7
occ:1.00
O A:GLU161 2.3 18.4 1.0
O A:HOH618 2.4 41.1 1.0
O A:HOH554 2.4 38.2 1.0
O A:HOH557 2.7 28.4 1.0
C A:GLU161 3.5 15.7 1.0
HA A:MET162 3.5 18.8 0.3
HA A:MET162 3.6 17.4 0.7
HB3 A:GLU161 4.0 20.3 1.0
HA A:GLU161 4.1 17.9 1.0
HD3 A:PRO163 4.2 20.1 1.0
HG3 A:MET162 4.3 24.3 0.3
N A:MET162 4.3 14.4 1.0
CA A:GLU161 4.3 14.9 1.0
CA A:MET162 4.4 15.6 0.3
CA A:MET162 4.4 14.5 0.7
OE2 A:GLU115 4.6 26.9 0.7
CB A:GLU161 4.7 16.9 1.0
OE1 A:GLU161 4.8 30.6 1.0
HD2 A:PRO163 4.9 20.1 1.0
HG2 A:MET162 4.9 16.8 0.7
CD A:PRO163 5.0 16.7 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: Mon Dec 14 20:51:39 2020

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