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Sodium in PDB 4qya: Crystal Structure of Human Transthyretin Variant V30M in Complex with Luteolin

Protein crystallography data

The structure of Crystal Structure of Human Transthyretin Variant V30M in Complex with Luteolin, PDB code: 4qya was solved by A.Begum, A.Olofsson, A.E.Sauer-Eriksson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 23.81 / 1.70
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 42.894, 85.854, 63.685, 90.00, 90.00, 90.00
R / Rfree (%) 16.3 / 19.8

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of Human Transthyretin Variant V30M in Complex with Luteolin (pdb code 4qya). 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 Transthyretin Variant V30M in Complex with Luteolin, PDB code: 4qya:

Sodium binding site 1 out of 1 in 4qya

Go back to Sodium Binding Sites List in 4qya
Sodium binding site 1 out of 1 in the Crystal Structure of Human Transthyretin Variant V30M in Complex with Luteolin


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 Transthyretin Variant V30M in Complex with Luteolin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na202

b:38.3
occ:1.00
O A:HOH391 2.2 32.7 1.0
O A:HOH333 2.2 31.9 1.0
O A:HOH398 2.3 17.6 1.0
O A:ASP99 2.5 26.1 1.0
O A:HOH344 2.7 31.6 1.0
C A:ASP99 3.7 28.4 1.0
OD1 A:ASP99 3.8 61.6 1.0
OE2 A:GLU66 4.1 24.4 1.0
O A:HOH401 4.2 36.4 0.5
CA A:ASP99 4.5 29.4 1.0
O A:HOH358 4.5 40.0 1.0
CD A:GLU66 4.7 27.7 1.0
OE1 A:GLU66 4.7 19.7 1.0
N A:SER100 4.7 23.1 1.0
CG A:ASP99 4.8 56.3 1.0
CA A:SER100 4.9 27.7 1.0

Reference:

I.Iakovleva, A.Begum, M.Pokrzywa, M.Walfridsson, A.E.Sauer-Eriksson, A.Olofsson. The Flavonoid Luteolin, But Not Luteolin-7-O-Glucoside, Prevents A Transthyretin Mediated Toxic Response. Plos One V. 10 28222 2015.
ISSN: ESSN 1932-6203
PubMed: 26020516
DOI: 10.1371/JOURNAL.PONE.0128222
Page generated: Tue Dec 15 07:06:58 2020

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