Potassium in PDB 3tze: Crystal Structure of A Tryptophanyl-Trna Synthetase From Encephalitozoon Cuniculi Bound to Tryptophan

All present enzymatic activity of Crystal Structure of A Tryptophanyl-Trna Synthetase From Encephalitozoon Cuniculi Bound to Tryptophan:
6.1.1.2;

The structure of Crystal Structure of A Tryptophanyl-Trna Synthetase From Encephalitozoon Cuniculi Bound to Tryptophan, PDB code: 3tze was solved by Seattle Structural Genomics Center For Infectious Disease (Ssgcid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.60
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	54.110, 79.160, 177.010, 90.00, 90.00, 90.00
R / Rfree (%)	20.2 / 24.7

The binding sites of Potassium atom in the Crystal Structure of A Tryptophanyl-Trna Synthetase From Encephalitozoon Cuniculi Bound to Tryptophan (pdb code 3tze). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Crystal Structure of A Tryptophanyl-Trna Synthetase From Encephalitozoon Cuniculi Bound to Tryptophan, PDB code: 3tze:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Crystal Structure of A Tryptophanyl-Trna Synthetase From Encephalitozoon Cuniculi Bound to Tryptophan


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Crystal Structure of A Tryptophanyl-Trna Synthetase From Encephalitozoon Cuniculi Bound to Tryptophan within 5.0Å range: probe atom residue distance (Å) B Occ A:K387 b:73.7 occ:1.00 O A:ILE218 2.6 49.9 1.0 O A:PHE215 3.1 37.7 1.0 O A:SER212 3.2 33.4 1.0 CA A:SER213 3.7 34.6 1.0 C A:ILE218 3.8 50.7 1.0 C A:SER212 3.8 33.7 1.0 N A:SER213 4.1 33.4 1.0 O A:ARG216 4.1 44.0 1.0 O A:GLY219 4.1 63.9 1.0 C A:PHE215 4.1 37.7 1.0 N A:ILE218 4.3 46.7 1.0 C A:GLY219 4.3 63.6 1.0 C A:ARG216 4.4 42.2 1.0 O A:LYS220 4.4 63.8 1.0 CA A:ARG216 4.5 42.0 1.0 C A:SER213 4.5 35.0 1.0 OG A:SER212 4.5 36.1 1.0 CA A:ILE218 4.5 46.3 1.0 CA A:LYS220 4.5 61.0 1.0 N A:LYS220 4.6 63.4 1.0 O A:SER213 4.7 36.3 1.0 CB A:SER213 4.7 34.4 1.0 N A:ARG216 4.7 40.1 1.0 CB A:ILE218 4.7 44.8 1.0 CB A:SER212 4.8 35.4 1.0 C A:LYS220 4.8 58.5 1.0 N A:GLY219 4.8 57.4 1.0 CA A:SER212 4.9 33.8 1.0

Potassium binding site 2 out of 2 in the Crystal Structure of A Tryptophanyl-Trna Synthetase From Encephalitozoon Cuniculi Bound to Tryptophan


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Crystal Structure of A Tryptophanyl-Trna Synthetase From Encephalitozoon Cuniculi Bound to Tryptophan within 5.0Å range: probe atom residue distance (Å) B Occ B:K387 b:59.3 occ:1.00 O B:ILE218 2.5 49.6 1.0 O B:PHE215 3.0 40.5 1.0 O B:SER212 3.1 36.8 1.0 C B:ILE218 3.7 49.1 1.0 C B:SER212 3.8 38.2 1.0 O B:GLY219 4.0 54.6 1.0 CA B:SER213 4.0 37.9 1.0 C B:PHE215 4.2 40.8 1.0 N B:SER213 4.2 37.9 1.0 C B:GLY219 4.2 53.5 1.0 OG B:SER212 4.3 41.8 1.0 CA B:LYS220 4.4 54.4 1.0 CA B:ILE218 4.4 47.6 1.0 N B:ILE218 4.4 47.6 1.0 O B:ARG216 4.5 47.1 1.0 N B:LYS220 4.6 55.0 1.0 CB B:ILE218 4.6 45.8 1.0 C B:SER213 4.6 36.7 1.0 CB B:SER212 4.7 39.3 1.0 C B:ARG216 4.7 45.8 1.0 N B:GLY219 4.7 49.9 1.0 CA B:ARG216 4.8 44.0 1.0 CA B:SER212 4.8 37.8 1.0 O B:SER213 4.9 35.8 1.0 CA B:GLY219 4.9 50.5 1.0 N B:ARG216 4.9 42.6 1.0 N B:PHE215 4.9 37.3 1.0 CG2 B:ILE218 5.0 44.0 1.0

S.O.Moen, T.E.Edwards, D.M.Dranow, M.C.Clifton, B.Sankaran, W.C.Van Voorhis, A.Sharma, C.Manoil, B.L.Staker, P.J.Myler, D.D.Lorimer. Ligand Co-Crystallization of Aminoacyl-Trna Synthetases From Infectious Disease Organisms. Sci Rep V. 7 223 2017.
ISSN: ESSN 2045-2322
PubMed: 28303005
DOI: 10.1038/S41598-017-00367-6