Magnesium in PDB 7bm9: Crystal Structure of 14-3-3 Sigma in Complex with CIP2APS904 Peptide

The structure of Crystal Structure of 14-3-3 Sigma in Complex with CIP2APS904 Peptide, PDB code: 7bm9 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)	41.86 / 1.80
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	82.554, 112.317, 62.809, 90, 90, 90
R / Rfree (%)	13.9 / 18.7

The structure of Crystal Structure of 14-3-3 Sigma in Complex with CIP2APS904 Peptide also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Magnesium atom in the Crystal Structure of 14-3-3 Sigma in Complex with CIP2APS904 Peptide (pdb code 7bm9). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of 14-3-3 Sigma in Complex with CIP2APS904 Peptide, PDB code: 7bm9:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of 14-3-3 Sigma in Complex with CIP2APS904 Peptide


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 14-3-3 Sigma in Complex with CIP2APS904 Peptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg302 b:2.4 occ:0.50 O A:HOH691 2.4 35.2 1.0 OE1 A:GLU2 2.4 7.5 1.0 O A:HOH452 2.5 5.0 1.0 CD A:GLU2 3.4 7.4 1.0 OE2 A:GLU2 3.8 6.6 1.0 HA A:GLU2 3.9 4.0 1.0 H A:ARG3 4.2 2.5 1.0 O A:HOH658 4.3 6.4 1.0 O A:HOH849 4.5 6.5 1.0 HB3 A:GLU2 4.6 5.2 1.0 CG A:GLU2 4.7 3.5 1.0 CA A:GLU2 4.8 3.3 1.0 CB A:GLU2 4.9 4.4 1.0 N A:ARG3 4.9 2.2 1.0 HG2 A:GLU2 5.0 4.2 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of 14-3-3 Sigma in Complex with CIP2APS904 Peptide


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of 14-3-3 Sigma in Complex with CIP2APS904 Peptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg303 b:5.1 occ:1.00 O A:GLU110 2.3 6.9 1.0 O A:HOH703 2.4 12.3 1.0 O A:HOH570 2.4 16.8 1.0 OE2 A:GLU35 2.5 9.5 1.0 OE1 A:GLU35 2.6 13.6 1.0 CD A:GLU35 2.9 15.9 1.0 H A:GLY112 3.5 9.3 1.0 C A:GLU110 3.6 9.4 1.0 HB3 A:GLU110 3.8 13.9 1.0 HA A:ALA111 3.9 5.5 1.0 N A:GLY112 4.1 7.8 1.0 O A:HOH713 4.1 22.3 1.0 HA A:GLU110 4.3 4.3 1.0 CG A:GLU35 4.4 8.1 1.0 HA3 A:GLY112 4.4 8.3 1.0 CA A:GLU110 4.4 3.6 1.0 N A:ALA111 4.5 3.5 1.0 O A:HOH554 4.5 14.3 1.0 CA A:ALA111 4.5 4.7 1.0 CB A:GLU110 4.6 11.6 1.0 HG2 A:GLU35 4.6 9.7 1.0 OE1 A:GLU110 4.6 28.8 1.0 O A:HOH433 4.6 26.6 1.0 C A:ALA111 4.7 7.4 1.0 O A:HOH524 4.8 14.3 1.0 HG3 A:GLU35 4.8 9.7 1.0 O A:HOH714 4.8 22.2 1.0 CA A:GLY112 4.9 6.9 1.0

H.J.Brink, J.R.Van Senten, I.J.De Vries-Van Leeuwen, D.Da Costa Pereira, S.R.Piersma, C.R.Jimenez, F.Centorrino, C.Ottmann, M.Siderius, M.J.Smit, A.H.De Boer. Fusicoccin-A Targets Cancerous Inhibitor of Protein Phosphatase 2A By Stabilizing A C-Terminal Interaction with 14-3-3. Acs Chem.Biol. V. 17 2972 2022.
ISSN: ESSN 1554-8937
PubMed: 36255265
DOI: 10.1021/ACSCHEMBIO.2C00299