Atomistry » Magnesium » PDB 8acg-8aom » 8alr
Atomistry »
  Magnesium »
    PDB 8acg-8aom »
      8alr »

Magnesium in PDB 8alr: Small Molecular Stabilizer For Eralpha and 14-3-3 (1080272)

Protein crystallography data

The structure of Small Molecular Stabilizer For Eralpha and 14-3-3 (1080272), PDB code: 8alr was solved by E.J.Visser, E.M.F.Vandenboorn, C.Ottmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.42 / 1.40
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 81.735, 112.169, 62.445, 90, 90, 90
R / Rfree (%) 14.8 / 17.1

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Small Molecular Stabilizer For Eralpha and 14-3-3 (1080272) (pdb code 8alr). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Small Molecular Stabilizer For Eralpha and 14-3-3 (1080272), PDB code: 8alr:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 8alr

Go back to Magnesium Binding Sites List in 8alr
Magnesium binding site 1 out of 2 in the Small Molecular Stabilizer For Eralpha and 14-3-3 (1080272)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Small Molecular Stabilizer For Eralpha and 14-3-3 (1080272) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg301

b:38.1
occ:1.00
O A:HOH643 3.1 37.4 1.0
O A:HOH426 3.4 15.1 1.0
O A:HOH417 4.2 23.8 1.0
O A:HOH591 4.3 27.2 1.0
O A:HOH646 4.4 29.7 1.0
NZ A:LYS159 4.5 35.0 1.0
OE2 A:GLU189 4.9 15.9 1.0

Magnesium binding site 2 out of 2 in 8alr

Go back to Magnesium Binding Sites List in 8alr
Magnesium binding site 2 out of 2 in the Small Molecular Stabilizer For Eralpha and 14-3-3 (1080272)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Small Molecular Stabilizer For Eralpha and 14-3-3 (1080272) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg302

b:24.4
occ:1.00
O A:HOH449 1.9 28.1 1.0
O A:HOH558 2.1 47.0 1.0
O A:HOH629 2.3 35.5 1.0
OE2 A:GLU89 2.4 16.3 1.0
CD A:GLU89 3.4 12.7 1.0
O A:HOH501 3.9 35.0 1.0
CG A:GLU89 4.2 11.6 1.0
OE1 A:GLU89 4.3 12.6 1.0
O A:HOH529 4.4 30.7 1.0
NH1 A:ARG85 4.5 15.0 1.0
OE1 A:GLN93 4.5 13.5 1.0
O A:HOH618 4.5 37.9 1.0
CG A:GLU86 4.7 15.2 1.0
NE2 A:GLN93 4.7 15.2 1.0
CB A:GLU89 4.8 11.6 1.0
OG1 A:THR90 4.9 17.3 1.0
CD A:GLN93 5.0 12.9 1.0

Reference:

M.Konstantinidou, E.J.Visser, E.Vandenboorn, S.Chen, P.Jaishankar, M.Overmans, S.Dutta, R.J.Neitz, A.R.Renslo, C.Ottmann, L.Brunsveld, M.R.Arkin. Structure-Based Optimization of Covalent, Small-Molecule Stabilizers of the 14-3-3 Sigma /Er Alpha Protein-Protein Interaction From Nonselective Fragments. J.Am.Chem.Soc. 2023.
ISSN: ESSN 1520-5126
PubMed: 37676236
DOI: 10.1021/JACS.3C05161
Page generated: Thu Oct 3 18:08:56 2024

Last articles

Mg in 4X1Y
Mg in 4X1K
Mg in 4X1I
Mg in 4X0Q
Mg in 4X0F
Mg in 4X0U
Mg in 4X04
Mg in 4WZA
Mg in 4WZB
Mg in 4WZI
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy