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Potassium in PDB 5e3a: Structure of Human DPP3 in Complex with Opioid Peptide Leu-Enkephalin

Enzymatic activity of Structure of Human DPP3 in Complex with Opioid Peptide Leu-Enkephalin

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

Protein crystallography data

The structure of Structure of Human DPP3 in Complex with Opioid Peptide Leu-Enkephalin, PDB code: 5e3a 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) 39.58 / 2.05
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 119.558, 105.757, 64.992, 90.00, 93.43, 90.00
R / Rfree (%) 20.9 / 26

Other elements in 5e3a:

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

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

Potassium Binding Sites:

The binding sites of Potassium atom in the Structure of Human DPP3 in Complex with Opioid Peptide Leu-Enkephalin (pdb code 5e3a). 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 Opioid Peptide Leu-Enkephalin, PDB code: 5e3a:

Potassium binding site 1 out of 1 in 5e3a

Go back to Potassium Binding Sites List in 5e3a
Potassium binding site 1 out of 1 in the Structure of Human DPP3 in Complex with Opioid Peptide Leu-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 Opioid Peptide Leu-Enkephalin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K804

b:29.0
occ:1.00
 O A:GLY323 2.7 23.2 1.0
OG A:SER504 2.7 26.9 1.0
OG A:SER317 2.9 26.8 1.0
O A:HOH901 2.9 28.1 1.0
O A:HOH933 2.9 21.2 1.0
OD1 A:ASP496 2.9 30.1 1.0
O A:SER317 3.2 30.0 1.0
O A:HOH1117 3.4 29.6 1.0
CG A:ASP496 3.5 30.4 1.0
C A:GLY323 3.6 22.4 1.0
O A:HOH908 3.6 33.9 1.0
CB A:SER317 3.6 27.4 1.0
N A:SER504 3.7 26.2 1.0
CB A:SER504 3.7 32.4 1.0
CA A:GLY323 3.9 23.6 1.0
CB A:ALA503 3.9 28.7 1.0
OD2 A:ASP496 3.9 30.8 1.0
C A:SER317 3.9 24.5 1.0
CA A:SER504 4.1 29.3 1.0
O A:SER500 4.3 29.9 1.0
CA A:SER317 4.4 29.5 1.0
C A:ALA503 4.4 27.7 1.0
CB A:ASP496 4.5 27.1 1.0
CA A:ALA503 4.7 28.9 1.0
N A:SER324 4.8 21.2 1.0
O A:HOH916 4.9 32.8 1.0
O A:HOH1124 4.9 30.2 1.0
N A:TYR318 4.9 23.9 1.0
CA A:ASP496 5.0 31.8 1.0
N A:SER317 5.0 27.0 1.0

Reference:

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
Page generated: Mon Aug 12 13:20:03 2024

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