Magnesium in PDB 7q26: Crystal Structure of Angiotensin-1 Converting Enzyme N-Domain in Complex with Dual Ace/Nep Inhibitor AD013

All present enzymatic activity of Crystal Structure of Angiotensin-1 Converting Enzyme N-Domain in Complex with Dual Ace/Nep Inhibitor AD013:
3.4.15.1;

The structure of Crystal Structure of Angiotensin-1 Converting Enzyme N-Domain in Complex with Dual Ace/Nep Inhibitor AD013, PDB code: 7q26 was solved by G.E.Cozier, K.R.Acharya, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	55.27 / 1.70
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	72.888, 77.1, 82.621, 88.63, 64.18, 74.79
R / Rfree (%)	19.5 / 21.5

The structure of Crystal Structure of Angiotensin-1 Converting Enzyme N-Domain in Complex with Dual Ace/Nep Inhibitor AD013 also contains other interesting chemical elements:

Zinc	(Zn)	2 atoms
Chlorine	(Cl)	2 atoms

The binding sites of Magnesium atom in the Crystal Structure of Angiotensin-1 Converting Enzyme N-Domain in Complex with Dual Ace/Nep Inhibitor AD013 (pdb code 7q26). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of Angiotensin-1 Converting Enzyme N-Domain in Complex with Dual Ace/Nep Inhibitor AD013, PDB code: 7q26:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Angiotensin-1 Converting Enzyme N-Domain in Complex with Dual Ace/Nep Inhibitor AD013


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Angiotensin-1 Converting Enzyme N-Domain in Complex with Dual Ace/Nep Inhibitor AD013 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg704 b:35.2 occ:1.00 OD1 A:ASN263 2.1 37.2 1.0 O A:HOH1079 2.4 38.4 1.0 OE2 A:GLU262 2.4 39.8 1.0 OD2 A:ASP354 2.4 38.9 1.0 O A:HOH974 2.4 34.7 1.0 OE1 A:GLU262 2.6 40.8 1.0 CD A:GLU262 2.9 41.6 1.0 O A:HOH1129 2.9 43.4 1.0 CG A:ASN263 3.2 36.5 1.0 HD22 A:ASN263 3.5 44.3 1.0 CG A:ASP354 3.6 37.7 1.0 HA A:ASN263 3.7 36.6 1.0 ND2 A:ASN263 3.7 36.9 1.0 HB3 A:ASP354 3.8 40.9 1.0 HB A:THR352 3.9 37.9 1.0 H A:ASP354 4.1 34.3 1.0 HG1 A:THR280 4.1 42.4 1.0 HG1 A:THR352 4.2 35.7 1.0 O A:HOH1013 4.2 35.8 1.0 CB A:ASP354 4.3 34.1 1.0 HB1 A:ALA148 4.3 50.9 1.0 CB A:ASN263 4.4 34.1 1.0 CG A:GLU262 4.4 34.1 1.0 CA A:ASN263 4.4 30.5 1.0 OD1 A:ASP354 4.5 45.0 1.0 HD21 A:ASN263 4.6 44.3 1.0 HG21 A:THR352 4.6 38.0 1.0 CB A:THR352 4.7 31.6 1.0 HG2 A:GLU262 4.7 40.9 1.0 OG1 A:THR352 4.7 29.8 1.0 N A:ASN263 4.7 28.9 1.0 HG3 A:GLU262 4.8 40.9 1.0 HB3 A:ASN263 4.8 40.9 1.0 O A:HOH921 4.9 42.6 1.0 OG1 A:THR280 4.9 35.3 1.0 N A:ASP354 4.9 28.6 1.0 HB2 A:ASP354 4.9 40.9 1.0 HB2 A:GLU262 5.0 34.4 1.0 H A:ASN263 5.0 34.7 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Angiotensin-1 Converting Enzyme N-Domain in Complex with Dual Ace/Nep Inhibitor AD013


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Angiotensin-1 Converting Enzyme N-Domain in Complex with Dual Ace/Nep Inhibitor AD013 within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg707 b:40.9 occ:1.00 O B:HOH828 2.0 34.3 1.0 OE2 B:GLU262 2.0 43.4 1.0 O B:HOH962 2.5 39.6 1.0 O B:HOH1083 2.5 38.8 1.0 HD22 B:ASN263 2.6 39.8 1.0 OD2 B:ASP354 2.9 48.9 1.0 ND2 B:ASN263 3.1 33.2 1.0 CD B:GLU262 3.2 40.6 1.0 HD21 B:ASN263 3.4 39.8 1.0 HG B:SER260 3.7 44.3 1.0 CG B:ASP354 3.7 38.5 1.0 HB2 B:ASP354 3.8 35.0 1.0 HG2 B:GLU262 3.9 41.1 1.0 OG B:SER260 4.0 37.0 1.0 CG B:ASN263 4.0 34.1 1.0 CG B:GLU262 4.0 34.2 1.0 HB3 B:ASP354 4.1 35.0 1.0 OE1 B:GLU262 4.1 36.0 1.0 CB B:ASP354 4.1 29.2 1.0 HG3 B:GLU262 4.2 41.1 1.0 O B:HOH1105 4.2 40.0 1.0 O B:HOH876 4.2 26.4 1.0 O B:HOH1024 4.3 41.0 1.0 O B:HOH1025 4.3 36.0 1.0 OD1 B:ASN263 4.3 34.1 1.0 HB2 B:ASP255 4.4 31.9 1.0 OD2 B:ASP255 4.5 30.4 1.0 O B:HOH1091 4.5 40.0 1.0 OD1 B:ASP354 4.7 41.5 1.0 O B:HOH961 4.9 27.4 1.0 H B:ASN263 4.9 31.4 1.0 O B:GLY254 5.0 27.5 1.0 O B:HOH822 5.0 28.6 1.0

L.B.Arendse, G.E.Cozier, C.J.Eyermann, G.S.Basarab, S.L.Schwager, K.Chibale, K.R.Acharya, E.D.Sturrock. Probing the Requirements For Dual Angiotensin-Converting Enzyme C-Domain Selective/Neprilysin Inhibition. J.Med.Chem. V. 65 3371 2022.
ISSN: ISSN 0022-2623
PubMed: 35113565
DOI: 10.1021/ACS.JMEDCHEM.1C01924