Sodium in PDB 4tls: Crystal Structure of Human Transthyretin GLU92PRO Mutant

The structure of Crystal Structure of Human Transthyretin GLU92PRO Mutant, PDB code: 4tls was solved by L.Saelices, D.Cascio, M.Sawaya, D.S.Eisenberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	64.36 / 1.35
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	42.380, 86.080, 64.360, 90.00, 90.00, 90.00
R / Rfree (%)	18.5 / 19.2

The binding sites of Sodium atom in the Crystal Structure of Human Transthyretin GLU92PRO Mutant (pdb code 4tls). 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 GLU92PRO Mutant, PDB code: 4tls:

Sodium binding site 1 out of 1 in the Crystal Structure of Human Transthyretin GLU92PRO Mutant


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 GLU92PRO Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Na202 b:33.8 occ:1.00 O B:LEU12 2.9 22.3 1.0 O B:THR59 3.1 22.7 1.0 N B:THR59 3.1 18.5 1.0 N B:LEU12 3.4 18.2 1.0 SG B:CYS10 3.5 20.0 1.0 N B:LEU58 3.5 19.3 1.0 CD B:PRO11 3.6 25.1 1.0 O B:HOH336 3.6 20.5 1.0 N B:PRO11 3.7 21.6 1.0 CG2 B:THR59 3.7 21.5 1.0 C B:THR59 3.7 22.1 1.0 C B:LEU12 3.8 20.2 1.0 CA B:CYS10 3.8 30.0 1.0 CA B:THR59 3.9 19.4 1.0 C B:CYS10 3.9 30.0 1.0 CA B:LEU12 4.0 17.2 1.0 C B:LEU58 4.1 21.2 1.0 C B:GLY57 4.1 21.9 1.0 CA B:LEU58 4.1 18.2 1.0 N B:GLY57 4.2 21.5 1.0 CB B:LEU58 4.2 17.4 1.0 CA B:GLY57 4.2 21.2 1.0 CB B:CYS10 4.2 20.0 1.0 CB B:LEU12 4.2 17.0 1.0 CG B:PRO11 4.4 28.3 1.0 CB B:THR59 4.4 20.2 1.0 C B:PRO11 4.4 19.9 1.0 CA B:PRO11 4.6 20.4 1.0 O B:CYS10 4.7 30.0 1.0 N B:THR60 4.8 21.7 1.0 N B:MET13 4.9 17.1 1.0 O B:GLY57 4.9 22.4 1.0

L.Saelices, L.M.Johnson, W.Y.Liang, M.R.Sawaya, D.Cascio, P.Ruchala, J.Whitelegge, L.Jiang, R.Riek, D.S.Eisenberg. Uncovering the Mechanism of Aggregation of Human Transthyretin. J.Biol.Chem. V. 290 28932 2015.
ISSN: ESSN 1083-351X
PubMed: 26459562
DOI: 10.1074/JBC.M115.659912