Potassium in PDB 5e33: Structure of Human DPP3 in Complex with Met-Enkephalin

All present enzymatic activity of Structure of Human DPP3 in Complex with Met-Enkephalin:
3.4.14.4;

The structure of Structure of Human DPP3 in Complex with Met-Enkephalin, PDB code: 5e33 was solved by P.Kumar, V.Reithofer, M.Reisinger, T.Pavkov-Keller, S.Wallner, P.Macheroux, K.Gruber, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.42 / 1.84
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	119.790, 105.760, 65.167, 90.00, 93.49, 90.00
R / Rfree (%)	18.2 / 22.4

The structure of Structure of Human DPP3 in Complex with Met-Enkephalin also contains other interesting chemical elements:

Magnesium	(Mg)	2 atoms
Zinc	(Zn)	1 atom

The binding sites of Potassium atom in the Structure of Human DPP3 in Complex with Met-Enkephalin (pdb code 5e33). 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 Structure of Human DPP3 in Complex with Met-Enkephalin, PDB code: 5e33:

Potassium binding site 1 out of 1 in the Structure of Human DPP3 in Complex with Met-Enkephalin


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Structure of Human DPP3 in Complex with Met-Enkephalin within 5.0Å range: probe atom residue distance (Å) B Occ A:K804 b:27.6 occ:1.00 O A:GLY323 2.6 24.2 1.0 OG A:SER504 2.7 25.0 1.0 OG A:SER317 2.7 24.4 1.0 OD1 A:ASP496 2.9 29.9 1.0 O A:SER317 3.0 22.4 1.0 O A:HOH1009 3.0 26.5 1.0 CG A:ASP496 3.5 29.7 1.0 C A:GLY323 3.5 27.3 1.0 CB A:SER317 3.6 28.9 1.0 O A:HOH1128 3.7 27.8 1.0 C A:SER317 3.7 28.3 1.0 CB A:SER504 3.8 24.8 1.0 O A:HOH1232 3.8 36.0 1.0 N A:SER504 3.8 25.5 1.0 OD2 A:ASP496 3.8 31.0 1.0 CA A:GLY323 3.9 26.8 1.0 CB A:ALA503 4.0 28.7 1.0 O A:HOH1018 4.0 27.8 1.0 CA A:SER504 4.2 23.6 1.0 CA A:SER317 4.3 23.5 1.0 CB A:ASP496 4.5 26.2 1.0 O A:SER500 4.5 28.6 1.0 C A:ALA503 4.6 24.5 1.0 N A:TYR318 4.7 24.0 1.0 N A:SER324 4.7 24.9 1.0 CA A:ALA503 4.8 26.0 1.0 O A:HOH996 4.9 25.6 1.0 N A:SER317 4.9 23.6 1.0 CA A:ASP496 5.0 26.7 1.0

P.Kumar, V.Reithofer, M.Reisinger, S.Wallner, T.Pavkov-Keller, P.Macheroux, K.Gruber. Substrate Complexes of Human Dipeptidyl Peptidase III Reveal the Mechanism of Enzyme Inhibition. Sci Rep V. 6 23787 2016.
ISSN: ESSN 2045-2322
PubMed: 27025154
DOI: 10.1038/SREP23787