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Magnesium in PDB 5e2q: Structure of Human DPP3 in Complex with Angiotensin-II

Enzymatic activity of Structure of Human DPP3 in Complex with Angiotensin-II

All present enzymatic activity of Structure of Human DPP3 in Complex with Angiotensin-II:
3.4.14.4;

Protein crystallography data

The structure of Structure of Human DPP3 in Complex with Angiotensin-II, PDB code: 5e2q was solved by P.Kumar, M.Reisinger, V.Reithofer, K.Gruber, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.33 / 2.40
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 119.131, 105.922, 64.846, 90.00, 93.91, 90.00
R / Rfree (%) 20.6 / 24.7

Other elements in 5e2q:

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

Potassium (K) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of Human DPP3 in Complex with Angiotensin-II (pdb code 5e2q). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Structure of Human DPP3 in Complex with Angiotensin-II, PDB code: 5e2q:

Magnesium binding site 1 out of 1 in 5e2q

Go back to Magnesium Binding Sites List in 5e2q
Magnesium binding site 1 out of 1 in the Structure of Human DPP3 in Complex with Angiotensin-II


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Human DPP3 in Complex with Angiotensin-II within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg801

b:22.5
occ:1.00
O A:HOH1037 2.5 31.0 1.0
O A:GLY164 2.6 36.6 1.0
O A:GLY167 2.8 32.5 1.0
O A:HOH1028 2.8 32.0 1.0
O A:HOH958 2.9 24.7 1.0
O A:GLY162 3.1 22.3 1.0
C A:GLY167 3.6 30.9 1.0
C A:LEU163 3.7 27.0 1.0
N A:GLY164 3.8 28.6 1.0
C A:GLY164 3.8 41.2 1.0
CA A:LEU163 3.9 27.6 1.0
O A:GLY174 4.1 29.5 1.0
C A:GLY162 4.1 23.3 1.0
CG2 A:THR169 4.1 24.0 1.0
N A:THR169 4.2 28.9 1.0
CA A:ILE168 4.2 27.1 1.0
N A:ILE168 4.2 28.4 1.0
O A:LEU163 4.2 34.4 1.0
CA A:GLY164 4.4 34.7 1.0
C A:ILE168 4.5 27.1 1.0
N A:LEU163 4.5 29.8 1.0
CA A:GLY167 4.5 32.0 1.0
O A:HOH909 4.5 36.2 1.0
CA A:GLY174 4.7 27.1 1.0
N A:GLY167 4.7 40.2 1.0
C A:GLY174 4.8 25.9 1.0
O A:CYS176 4.8 31.1 1.0
N A:LYS165 4.9 40.2 1.0
CB A:THR169 5.0 20.9 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: Sun Sep 29 03:28:05 2024

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