Potassium in PDB 6htk: X-Ray Structure of the Tryptophan Lyase Nosl in Complex with (R)-(+)- Indoline-2-Carboxylate

The structure of X-Ray Structure of the Tryptophan Lyase Nosl in Complex with (R)-(+)- Indoline-2-Carboxylate, PDB code: 6htk was solved by P.Amara, J.M.Mouesca, M.Bella, L.Martin, C.Saragaglia, S.Gambarelli, Y.Nicolet, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.11 / 2.00
Space group	P 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	94.650, 47.010, 114.080, 90.00, 108.91, 90.00
R / Rfree (%)	16.9 / 19.7

The structure of X-Ray Structure of the Tryptophan Lyase Nosl in Complex with (R)-(+)- Indoline-2-Carboxylate also contains other interesting chemical elements:

Bromine	(Br)	6 atoms
Iron	(Fe)	8 atoms
Sodium	(Na)	2 atoms

The binding sites of Potassium atom in the X-Ray Structure of the Tryptophan Lyase Nosl in Complex with (R)-(+)- Indoline-2-Carboxylate (pdb code 6htk). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the X-Ray Structure of the Tryptophan Lyase Nosl in Complex with (R)-(+)- Indoline-2-Carboxylate, PDB code: 6htk:

Potassium binding site 1 out of 1 in the X-Ray Structure of the Tryptophan Lyase Nosl in Complex with (R)-(+)- Indoline-2-Carboxylate


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of X-Ray Structure of the Tryptophan Lyase Nosl in Complex with (R)-(+)- Indoline-2-Carboxylate within 5.0Å range: probe atom residue distance (Å) B Occ B:K513 b:74.6 occ:0.87 OD2 B:ASP33 2.8 49.6 1.0 OD1 B:ASP33 3.0 47.8 1.0 O B:HOH1055 3.2 54.1 1.0 CG B:ASP33 3.2 46.6 1.0 N B:ALA36 4.1 44.4 1.0 CB B:ALA36 4.1 44.1 1.0 CB B:ARG35 4.3 49.8 0.5 CB B:ARG35 4.3 49.8 0.5 CA B:ALA36 4.5 44.1 1.0 O B:HOH1038 4.5 60.1 1.0 O B:HOH655 4.6 46.5 1.0 C B:ARG35 4.6 44.1 1.0 CB B:ASP33 4.7 41.6 1.0 CG B:ARG35 4.9 52.8 0.5 CA B:ARG35 5.0 46.1 0.5 CA B:ARG35 5.0 46.2 0.5

P.Amara, J.M.Mouesca, M.Bella, L.Martin, C.Saragaglia, S.Gambarelli, Y.Nicolet. Radical S-Adenosyl-L-Methionine Tryptophan Lyase (Nosl): How the Protein Controls the Carboxyl Radical •CO2-Migration. J.Am.Chem.Soc. V. 140 16661 2018.
ISSN: ESSN 1520-5126
PubMed: 30418774
DOI: 10.1021/JACS.8B09142