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Sodium in PDB 6qbf: Crystal Structure of the Pathological D187N Variant of Calcium-Free Human Gelsolin.

Protein crystallography data

The structure of Crystal Structure of the Pathological D187N Variant of Calcium-Free Human Gelsolin., PDB code: 6qbf was solved by E.Scalone, F.Boni, M.Milani, M.Eloise, M.De Rosa, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 75.88 / 3.50
Space group P 4 21 2
Cell size a, b, c (Å), α, β, γ (°) 169.673, 169.673, 151.089, 90.00, 90.00, 90.00
R / Rfree (%) 21.8 / 27.6

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of the Pathological D187N Variant of Calcium-Free Human Gelsolin. (pdb code 6qbf). 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 the Pathological D187N Variant of Calcium-Free Human Gelsolin., PDB code: 6qbf:

Sodium binding site 1 out of 1 in 6qbf

Go back to Sodium Binding Sites List in 6qbf
Sodium binding site 1 out of 1 in the Crystal Structure of the Pathological D187N Variant of Calcium-Free Human Gelsolin.


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 the Pathological D187N Variant of Calcium-Free Human Gelsolin. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Na802

b:29.0
occ:1.00
NE1 B:TRP736 3.6 82.9 1.0
OE2 B:GLU725 3.7 80.1 1.0
OD1 B:ASP738 3.7 92.9 1.0
CA B:ASP738 4.1 82.9 1.0
O B:ASP738 4.1 91.3 1.0
O B:GLY723 4.3 78.4 1.0
NH2 B:ARG458 4.3 89.1 1.0
CE2 B:TRP736 4.3 72.4 1.0
CZ2 B:TRP736 4.3 74.1 1.0
CB B:ASP738 4.4 81.0 1.0
CG B:ASP738 4.5 91.3 1.0
C B:ASP738 4.6 89.0 1.0
C B:GLY723 4.6 72.0 1.0
CD1 B:TRP736 4.7 88.7 1.0
CD B:GLU725 4.7 74.3 1.0
CA B:GLY723 4.9 62.6 1.0
N B:GLU725 5.0 50.2 1.0

Reference:

M.De Rosa, A.Barbiroli, F.Boni, E.Scalone, D.Mattioni, M.A.Vanoni, M.Patrone, M.Bollati, E.Mastrangelo, T.Giorgino, M.Milani. The Structure of N184K Amyloidogenic Variant of Gelsolin Highlights the Role of the H-Bond Network For Protein Stability and Aggregation Properties. Eur.Biophys.J. 2019.
ISSN: ISSN 0175-7571
PubMed: 31724080
DOI: 10.1007/S00249-019-01409-9
Page generated: Tue Dec 15 12:48:44 2020

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