Potassium in PDB 5fht: HTRA2 Protease Mutant V226K

All present enzymatic activity of HTRA2 Protease Mutant V226K:
3.4.21.108;

The structure of HTRA2 Protease Mutant V226K, PDB code: 5fht was solved by P.Golik, G.Dubin, D.Zurawa-Janicka, B.Lipinska, M.Jarzab, T.Wenta, A.Gieldon, A.Ciarkowski, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	14.57 / 1.95
Space group	H 3
Cell size a, b, c (Å), α, β, γ (°)	86.010, 86.010, 126.700, 90.00, 90.00, 120.00
R / Rfree (%)	17.5 / 22.8

The structure of HTRA2 Protease Mutant V226K also contains other interesting chemical elements:

Chlorine	(Cl)	1 atom
Sodium	(Na)	1 atom

The binding sites of Potassium atom in the HTRA2 Protease Mutant V226K (pdb code 5fht). 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 HTRA2 Protease Mutant V226K, PDB code: 5fht:

Potassium binding site 1 out of 1 in the HTRA2 Protease Mutant V226K


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of HTRA2 Protease Mutant V226K within 5.0Å range: probe atom residue distance (Å) B Occ A:K403 b:34.9 occ:1.00 OG1 A:THR235 2.9 26.9 1.0 O A:HOH606 3.0 31.3 1.0 O A:HOH578 3.0 30.6 1.0 O A:HOH550 3.2 29.9 1.0 N A:VAL159 3.3 27.4 1.0 CA A:ASN158 3.8 31.8 1.0 CB A:THR235 3.8 30.0 1.0 CG2 A:VAL159 4.0 29.0 1.0 CB A:ASN158 4.0 32.6 1.0 C A:ASN158 4.1 31.8 1.0 CB A:VAL159 4.1 28.5 1.0 ND2 A:ASN158 4.2 34.3 1.0 CB A:ALA291 4.2 25.4 1.0 CA A:VAL159 4.3 27.3 1.0 CD A:LYS93 4.4 38.8 1.0 CG A:ASN158 4.4 34.2 1.0 CE A:LYS93 4.5 36.0 1.0 CG A:LYS93 4.5 37.9 1.0 N A:ALA291 4.6 26.0 1.0 O A:HOH620 4.7 31.5 1.0 CG2 A:THR235 4.7 29.5 1.0 OH A:TYR161 4.8 28.2 1.0 O A:VAL159 4.8 27.0 1.0 N A:THR235 4.9 28.0 1.0 NZ A:LYS93 4.9 39.7 1.0 CA A:ALA291 4.9 27.9 1.0 CA A:THR235 5.0 28.4 1.0

A.Gieldon, D.Zurawa-Janicka, M.Jarzab, T.Wenta, P.Golik, G.Dubin, B.Lipinska, J.Ciarkowski. Distinct 3D Architecture and Dynamics of the Human HTRA2(Omi) Protease and Its Mutated Variants. Plos One V. 11 61526 2016.
ISSN: ESSN 1932-6203
PubMed: 27571206
DOI: 10.1371/JOURNAL.PONE.0161526