Magnesium in PDB 3ux0: Crystal Structure of Human 14-3-3 Sigma in Complex with Task-3 Peptide and Stabilizer Fusicoccin H

The structure of Crystal Structure of Human 14-3-3 Sigma in Complex with Task-3 Peptide and Stabilizer Fusicoccin H, PDB code: 3ux0 was solved by P.Thiel, M.Bartel, C.Anders, Y.Higuchi, B.Schumacher, N.Kato, C.Ottmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.46 / 1.75
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	81.900, 111.040, 62.350, 90.00, 90.00, 90.00
R / Rfree (%)	15.1 / 19.2

The structure of Crystal Structure of Human 14-3-3 Sigma in Complex with Task-3 Peptide and Stabilizer Fusicoccin H also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Magnesium atom in the Crystal Structure of Human 14-3-3 Sigma in Complex with Task-3 Peptide and Stabilizer Fusicoccin H (pdb code 3ux0). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Crystal Structure of Human 14-3-3 Sigma in Complex with Task-3 Peptide and Stabilizer Fusicoccin H, PDB code: 3ux0:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in the Crystal Structure of Human 14-3-3 Sigma in Complex with Task-3 Peptide and Stabilizer Fusicoccin H


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 Human 14-3-3 Sigma in Complex with Task-3 Peptide and Stabilizer Fusicoccin H within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg232 b:12.9 occ:0.50 O A:HOH470 2.3 16.0 0.3 OE1 A:GLU2 2.4 21.0 1.0 O A:HOH350 2.6 17.0 1.0 O A:HOH470 2.7 36.7 0.7 CD A:GLU2 3.4 21.3 1.0 OE2 A:GLU2 3.8 20.9 1.0 O A:HOH551 4.2 51.3 1.0 O A:HOH352 4.4 14.0 1.0 O A:HOH387 4.4 19.7 1.0 CG A:GLU2 4.8 14.5 1.0 CA A:GLU2 4.9 13.0 1.0 N A:ARG3 4.9 12.2 1.0

Magnesium binding site 2 out of 4 in the Crystal Structure of Human 14-3-3 Sigma in Complex with Task-3 Peptide and Stabilizer Fusicoccin H


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 Human 14-3-3 Sigma in Complex with Task-3 Peptide and Stabilizer Fusicoccin H within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg233 b:13.1 occ:1.00 O A:HOH525 2.1 29.6 1.0 OE1 A:GLU35 2.3 23.3 1.0 O A:HOH473 2.3 37.2 1.0 O A:GLU110 2.3 16.5 1.0 O A:HOH474 2.4 24.3 1.0 OE2 A:GLU35 2.8 31.5 1.0 CD A:GLU35 2.9 25.5 1.0 C A:GLU110 3.5 15.7 1.0 N A:GLY112 4.0 19.1 1.0 CG A:GLU35 4.4 19.8 1.0 CA A:GLU110 4.4 15.7 0.6 CA A:GLU110 4.4 15.6 0.4 CB A:GLU110 4.5 15.7 0.6 N A:ALA111 4.5 14.7 1.0 CA A:ALA111 4.5 15.5 1.0 OE1 A:GLU110 4.6 18.5 0.6 O A:HOH459 4.6 32.2 1.0 O A:HOH257 4.7 37.5 1.0 C A:ALA111 4.7 17.9 1.0 CB A:GLU110 4.7 15.6 0.4 O A:HOH484 4.7 38.1 1.0 CA A:GLY112 4.7 20.6 1.0 O A:HOH526 4.7 41.1 1.0

Magnesium binding site 3 out of 4 in the Crystal Structure of Human 14-3-3 Sigma in Complex with Task-3 Peptide and Stabilizer Fusicoccin H


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of Human 14-3-3 Sigma in Complex with Task-3 Peptide and Stabilizer Fusicoccin H within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg234 b:41.7 occ:1.00 O A:HOH542 2.3 32.5 1.0 O A:HOH320 2.4 44.7 1.0 OE2 A:GLU89 2.4 22.7 1.0 OE2 A:GLU86 2.5 19.6 0.4 OE1 A:GLU86 2.6 21.4 0.4 CD A:GLU86 2.9 19.2 0.4 CD A:GLU89 3.5 16.4 1.0 O A:HOH541 4.0 32.8 1.0 CG A:GLU89 4.1 15.6 1.0 O A:HOH475 4.2 33.9 1.0 OE1 A:GLU89 4.3 16.6 1.0 CG A:GLU86 4.4 16.8 0.4 NH1 A:ARG85 4.5 21.0 1.0 OE1 A:GLN93 4.5 17.2 1.0 NE2 A:GLN93 4.7 16.2 1.0 CG A:GLU86 4.8 12.3 0.6 CB A:GLU89 4.8 13.7 1.0 OG1 A:THR90 5.0 18.6 1.0

Magnesium binding site 4 out of 4 in the Crystal Structure of Human 14-3-3 Sigma in Complex with Task-3 Peptide and Stabilizer Fusicoccin H


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Crystal Structure of Human 14-3-3 Sigma in Complex with Task-3 Peptide and Stabilizer Fusicoccin H within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg235 b:31.7 occ:1.00 O A:HOH325 2.0 38.4 1.0 O A:HOH314 2.2 50.4 1.0 O A:GLU161 2.3 20.7 1.0 O A:HOH301 2.5 44.1 1.0 C A:GLU161 3.5 18.6 1.0 CA A:MET162 4.3 17.7 1.0 N A:MET162 4.4 16.5 1.0 OE2 A:GLU115 4.4 25.4 0.5 CA A:GLU161 4.4 18.6 0.3 CA A:GLU161 4.4 18.5 0.7 CB A:GLU161 4.8 18.8 0.3 CB A:GLU161 4.8 19.1 0.7 CD A:PRO163 4.8 18.5 1.0 OE1 A:GLU161 4.9 25.0 0.7 O A:HOH270 4.9 48.1 1.0

C.Anders, Y.Higuchi, K.Koschinsky, M.Bartel, B.Schumacher, P.Thiel, H.Nitta, R.Preisig-Muller, G.Schlichthorl, V.Renigunta, J.Ohkanda, J.Daut, N.Kato, C.Ottmann. A Semisynthetic Fusicoccane Stabilizes A Protein-Protein Interaction and Enhances the Expression of K(+) Channels at the Cell Surface. Chem.Biol. V. 20 583 2013.
ISSN: ISSN 1074-5521
PubMed: 23601647
DOI: 10.1016/J.CHEMBIOL.2013.03.015