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Magnesium in PDB 3smk: Crystal Structure of Human 14-3-3 Sigma C38V/N166H in Complex with Task-3 Peptide and Stabilizer Cotylenin A

Protein crystallography data

The structure of Crystal Structure of Human 14-3-3 Sigma C38V/N166H in Complex with Task-3 Peptide and Stabilizer Cotylenin A, PDB code: 3smk was solved by C.Anders, B.Schumacher, C.Ottmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.34 / 2.10
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 81.290, 111.780, 63.110, 90.00, 90.00, 90.00
R / Rfree (%) 18.7 / 23.7

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Human 14-3-3 Sigma C38V/N166H in Complex with Task-3 Peptide and Stabilizer Cotylenin A (pdb code 3smk). 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 Human 14-3-3 Sigma C38V/N166H in Complex with Task-3 Peptide and Stabilizer Cotylenin A, PDB code: 3smk:

Magnesium binding site 1 out of 1 in 3smk

Go back to Magnesium Binding Sites List in 3smk
Magnesium binding site 1 out of 1 in the Crystal Structure of Human 14-3-3 Sigma C38V/N166H in Complex with Task-3 Peptide and Stabilizer Cotylenin 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 Human 14-3-3 Sigma C38V/N166H in Complex with Task-3 Peptide and Stabilizer Cotylenin A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg233

b:33.7
occ:1.00
O A:HOH235 2.3 27.3 1.0
NE2 A:HIS106 2.9 44.8 1.0
OE2 A:GLU31 3.1 33.5 1.0
CG A:GLU31 3.5 22.9 1.0
CD2 A:HIS106 3.6 42.3 1.0
CD A:GLU31 3.7 31.0 1.0
CE1 A:HIS106 4.0 43.8 1.0
CD2 A:LEU102 4.1 23.7 1.0
CB A:SER105 4.4 36.2 1.0
O A:HOH300 4.8 25.5 1.0
CG A:HIS106 4.8 41.4 1.0
OG A:SER105 4.8 39.4 1.0
OE1 A:GLU31 4.9 31.1 1.0
CB A:GLU31 4.9 17.7 1.0
ND1 A:HIS106 5.0 42.9 1.0

Reference:

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 1879-1301
PubMed: 23601647
DOI: 10.1016/J.CHEMBIOL.2013.03.015
Page generated: Thu Aug 15 11:04:28 2024

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