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Sodium in PDB 5myc: Crystal Structure of Human 14-3-3 Sigma in Complex with LRRK2 Peptide PS910

Enzymatic activity of Crystal Structure of Human 14-3-3 Sigma in Complex with LRRK2 Peptide PS910

All present enzymatic activity of Crystal Structure of Human 14-3-3 Sigma in Complex with LRRK2 Peptide PS910:
2.7.11.1;

Protein crystallography data

The structure of Crystal Structure of Human 14-3-3 Sigma in Complex with LRRK2 Peptide PS910, PDB code: 5myc was solved by L.M.Stevers, R.M.J.M.De Vries, C.Ottmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 41.85 / 1.46
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 82.517, 112.411, 62.689, 90.00, 90.00, 90.00
R / Rfree (%) 16.6 / 18.9

Other elements in 5myc:

The structure of Crystal Structure of Human 14-3-3 Sigma in Complex with LRRK2 Peptide PS910 also contains other interesting chemical elements:

Calcium (Ca) 2 atoms
Chlorine (Cl) 1 atom

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of Human 14-3-3 Sigma in Complex with LRRK2 Peptide PS910 (pdb code 5myc). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Crystal Structure of Human 14-3-3 Sigma in Complex with LRRK2 Peptide PS910, PDB code: 5myc:

Sodium binding site 1 out of 1 in 5myc

Go back to Sodium Binding Sites List in 5myc
Sodium binding site 1 out of 1 in the Crystal Structure of Human 14-3-3 Sigma in Complex with LRRK2 Peptide PS910


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of Human 14-3-3 Sigma in Complex with LRRK2 Peptide PS910 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na304

b:40.4
occ:1.00
 O A:HOH677 2.2 51.5 1.0
O A:HOH416 2.4 35.1 1.0
NZ A:LYS124 2.7 22.1 1.0
O A:HOH453 2.9 51.5 1.0
OE2 A:GLU153 3.5 22.9 0.3
CD2 A:LEU121 3.6 14.7 1.0
CE A:LYS124 3.6 17.4 1.0
CD A:LYS124 3.7 13.5 1.0
O A:HOH711 3.9 61.5 1.0
OE1 A:GLU153 4.0 24.5 0.7
O A:HOH739 4.1 49.9 1.0
CD A:GLU153 4.2 23.6 0.3
OE1 A:GLU153 4.2 27.5 0.3
O A:HOH547 4.5 24.8 1.0
CD1 A:ILE108 4.6 14.5 1.0
O A:HOH476 4.7 22.1 1.0
CG2 A:ILE108 4.8 12.3 1.0

Reference:

L.M.Stevers, R.M.De Vries, R.G.Doveston, L.G.Milroy, L.Brunsveld, C.Ottmann. Structural Interface Between LRRK2 and 14-3-3 Protein. Biochem. J. V. 474 1273 2017.
ISSN: ESSN 1470-8728
PubMed: 28202711
DOI: 10.1042/BCJ20161078
Page generated: Mon Oct 7 22:48:57 2024

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