Potassium in PDB 3s7k: Structure of Thrombin Mutant Y225P in the E Form

All present enzymatic activity of Structure of Thrombin Mutant Y225P in the E Form:
3.4.21.5;

The structure of Structure of Thrombin Mutant Y225P in the E Form, PDB code: 3s7k was solved by W.Niu, Z.Chen, P.Gandhi, A.Vogt, N.Pozzi, L.A.Pele, F.Zapata, E.Di Cera, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.67 / 1.90
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	61.937, 86.813, 100.968, 90.00, 90.00, 90.00
R / Rfree (%)	17.5 / 21.7

The binding sites of Potassium atom in the Structure of Thrombin Mutant Y225P in the E Form (pdb code 3s7k). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Structure of Thrombin Mutant Y225P in the E Form, PDB code: 3s7k:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Structure of Thrombin Mutant Y225P in the E Form


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Structure of Thrombin Mutant Y225P in the E Form within 5.0Å range: probe atom residue distance (Å) B Occ A:K402 b:20.4 occ:0.50 O B:HOH381 2.6 43.1 0.5 O A:TYR14J 2.7 20.5 1.0 OH B:TYR134 2.8 18.2 1.0 O A:HOH94 3.2 27.3 1.0 C A:TYR14J 3.7 20.1 1.0 CZ B:TYR134 3.8 17.4 1.0 CA A:ILE14K 4.0 25.0 1.0 O A:ILE14K 4.1 28.1 1.0 O B:HOH15 4.2 35.6 1.0 CE1 B:TYR134 4.3 17.7 1.0 N A:ILE14K 4.3 21.6 1.0 C A:ILE14K 4.3 28.1 1.0 CE2 B:TYR134 4.8 16.6 1.0 CA A:TYR14J 4.9 18.1 1.0

Potassium binding site 2 out of 2 in the Structure of Thrombin Mutant Y225P in the E Form


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Structure of Thrombin Mutant Y225P in the E Form within 5.0Å range: probe atom residue distance (Å) B Occ C:K402 b:20.8 occ:0.50 O C:TYR14J 2.6 21.4 1.0 OH D:TYR134 2.7 18.6 1.0 O D:HOH295 2.7 28.7 1.0 CZ D:TYR134 3.7 18.4 1.0 C C:TYR14J 3.8 22.4 1.0 O C:ILE14K 3.9 27.3 1.0 CE1 D:TYR134 4.1 16.1 1.0 CA C:ILE14K 4.2 26.4 1.0 O D:HOH3 4.2 35.0 1.0 C C:ILE14K 4.3 27.4 1.0 O C:HOH307 4.4 28.5 1.0 N C:ILE14K 4.5 22.9 1.0 CE2 D:TYR134 4.9 15.6 1.0 CA C:TYR14J 4.9 20.8 1.0

W.Niu, Z.Chen, P.S.Gandhi, A.D.Vogt, N.Pozzi, L.A.Pelc, F.Zapata, E.Di Cera. Crystallographic and Kinetic Evidence of Allostery in A Trypsin-Like Protease. Biochemistry V. 50 6301 2011.
ISSN: ISSN 0006-2960
PubMed: 21707111
DOI: 10.1021/BI200878C