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Sodium in PDB 4pmf: Human Transthyretin (Ttr) Complexed with Curcumin

Protein crystallography data

The structure of Human Transthyretin (Ttr) Complexed with Curcumin, PDB code: 4pmf 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) 39.00 / 1.35
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 43.255, 85.487, 64.168, 90.00, 90.00, 90.00
R / Rfree (%) 17.6 / 20.9

Sodium Binding Sites:

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

Sodium binding site 1 out of 1 in 4pmf

Go back to Sodium Binding Sites List in 4pmf
Sodium binding site 1 out of 1 in the Human Transthyretin (Ttr) Complexed with 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 Curcumin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na202

b:40.2
occ:1.00
O A:HOH328 2.3 29.9 1.0
O A:HOH354 2.3 44.7 1.0
O A:HOH341 2.3 29.6 1.0
O A:HOH301 2.8 34.2 1.0
O A:ASP99 2.9 26.0 0.6
O A:ASP99 3.2 27.6 0.4
C A:ASP99 3.9 28.0 0.6
N A:GLY101 3.9 22.6 1.0
C A:ASP99 3.9 28.0 0.4
CA A:SER100 4.1 27.7 0.6
CA A:SER100 4.2 27.9 0.4
C A:SER100 4.2 26.8 0.6
C A:SER100 4.2 26.8 0.4
N A:SER100 4.4 27.5 0.4
O A:HOH308 4.4 36.1 1.0
N A:SER100 4.4 27.2 0.6
OE1 A:GLU66 4.4 20.4 1.0
O A:ASN98 4.6 23.2 1.0
CD A:GLU66 4.7 25.5 1.0
CA A:GLY101 4.7 20.5 1.0
OE2 A:GLU66 4.8 22.5 1.0
CA A:ASP99 4.9 24.2 0.4
CA A:ASP99 5.0 24.0 0.6
O A:SER100 5.0 30.3 0.4

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: Mon Oct 7 17:44:50 2024

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