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Sodium in PDB 4pme: Human Transthyretin (Ttr) Complexed with Ferulic Acid and Curcumin.

Protein crystallography data

The structure of Human Transthyretin (Ttr) Complexed with Ferulic Acid and Curcumin., PDB code: 4pme was solved by E.A.Stura, L.Ciccone, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.34 / 1.26
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 42.990, 84.670, 64.060, 90.00, 90.00, 90.00
R / Rfree (%) 18.1 / 20.7

Sodium Binding Sites:

The binding sites of Sodium atom in the Human Transthyretin (Ttr) Complexed with Ferulic Acid and Curcumin. (pdb code 4pme). 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 Human Transthyretin (Ttr) Complexed with Ferulic Acid and Curcumin., PDB code: 4pme:

Sodium binding site 1 out of 1 in 4pme

Go back to Sodium Binding Sites List in 4pme
Sodium binding site 1 out of 1 in the Human Transthyretin (Ttr) Complexed with Ferulic Acid and Curcumin.


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Human Transthyretin (Ttr) Complexed with Ferulic Acid and Curcumin. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na202

b:39.9
occ:1.00
O A:ASP99 2.2 26.3 0.8
O A:HOH313 2.3 33.0 1.0
O A:ASP99 2.3 27.3 0.2
O A:HOH336 2.4 31.8 1.0
O A:HOH353 2.4 43.8 1.0
O A:HOH319 2.6 43.4 1.0
C A:ASP99 3.4 30.4 0.8
C A:ASP99 3.4 30.2 0.2
OD1 A:ASP99 3.5 39.8 0.8
CG A:ASP99 3.9 37.9 0.8
O A:HOH332 4.1 33.5 1.0
OD2 A:ASP99 4.2 40.6 0.8
CA A:ASP99 4.2 28.9 0.2
CA A:ASP99 4.2 28.7 0.8
OE2 A:GLU66 4.2 25.4 1.0
N A:SER100 4.4 29.2 1.0
CA A:SER100 4.6 30.0 1.0
CB A:ASP99 4.6 31.1 0.2
CB A:ASP99 4.7 30.5 0.8
CD A:GLU66 4.8 26.9 1.0
OE1 A:GLU66 4.8 23.1 1.0

Reference:

L.Ciccone, L.Tepshi, S.Nencetti, E.A.Stura. Transthyretin Complexes with Curcumin and Bromo-Estradiol: Evaluation of Solubilizing Multicomponent Mixtures. N Biotechnol V. 32 54 2014.
ISSN: ISSN 1876-4347
PubMed: 25224922
DOI: 10.1016/J.NBT.2014.09.002
Page generated: Tue Dec 15 06:58:27 2020

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