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Potassium in PDB 4rkj: Crystal Structure of Thrombin Mutant S195T (Free Form)

Enzymatic activity of Crystal Structure of Thrombin Mutant S195T (Free Form)

All present enzymatic activity of Crystal Structure of Thrombin Mutant S195T (Free Form):
3.4.21.5;

Protein crystallography data

The structure of Crystal Structure of Thrombin Mutant S195T (Free Form), PDB code: 4rkj was solved by A.L.Pelc, Z.Chen, D.W.Gohara, A.D.Vogt, N.Pozzi, E.Di Cera, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.00 / 1.70
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 61.415, 91.114, 50.553, 90.00, 90.00, 90.00
R / Rfree (%) 15.6 / 20.7

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of Thrombin Mutant S195T (Free Form) (pdb code 4rkj). 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 Crystal Structure of Thrombin Mutant S195T (Free Form), PDB code: 4rkj:

Potassium binding site 1 out of 1 in 4rkj

Go back to Potassium Binding Sites List in 4rkj
Potassium binding site 1 out of 1 in the Crystal Structure of Thrombin Mutant S195T (Free Form)


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 Thrombin Mutant S195T (Free Form) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K301

b:22.4
occ:0.50
O A:TYR14J 2.6 26.7 1.0
O B:HOH597 2.7 56.6 1.0
OH B:TYR134 2.8 22.5 1.0
O B:HOH598 3.3 61.6 1.0
CZ B:TYR134 3.8 22.3 1.0
C A:TYR14J 3.8 24.4 1.0
CE1 B:TYR134 4.1 23.5 1.0
O A:ILE14K 4.1 28.0 1.0
CA A:ILE14K 4.2 25.9 1.0
C A:ILE14K 4.4 26.6 1.0
N A:ILE14K 4.4 23.8 1.0
O B:HOH500 4.5 42.7 1.0
CA A:TYR14J 4.9 22.9 1.0
CE2 B:TYR134 4.9 19.4 1.0

Reference:

L.A.Pelc, Z.Chen, D.W.Gohara, A.D.Vogt, N.Pozzi, E.Di Cera. Why Ser and Not Thr Brokers Catalysis in the Trypsin Fold. Biochemistry V. 54 1457 2015.
ISSN: ISSN 0006-2960
PubMed: 25664608
DOI: 10.1021/ACS.BIOCHEM.5B00014
Page generated: Sat Aug 9 07:48:19 2025

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