Magnesium in PDB 7q25: Crystal Structure of Angiotensin-1 Converting Enzyme N-Domain in Complex with Dual Ace/Nep Inhibitor AD012

All present enzymatic activity of Crystal Structure of Angiotensin-1 Converting Enzyme N-Domain in Complex with Dual Ace/Nep Inhibitor AD012:
3.4.15.1;

The structure of Crystal Structure of Angiotensin-1 Converting Enzyme N-Domain in Complex with Dual Ace/Nep Inhibitor AD012, PDB code: 7q25 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)	63.17 / 1.60
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	72.935, 77.482, 82.489, 88.39, 64.24, 74.99
R / Rfree (%)	18.8 / 21.2

The structure of Crystal Structure of Angiotensin-1 Converting Enzyme N-Domain in Complex with Dual Ace/Nep Inhibitor AD012 also contains other interesting chemical elements:

Chlorine	(Cl)	2 atoms
Zinc	(Zn)	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 AD012 (pdb code 7q25). 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 AD012, PDB code: 7q25:
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 AD012


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 AD012 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg714 b:40.5 occ:1.00 OD1 A:ASN263 2.3 56.9 1.0 O A:HOH1063 2.3 36.5 1.0 O A:HOH974 2.5 33.4 1.0 OD2 A:ASP354 2.5 58.3 1.0 OE1 A:GLU262 2.8 74.8 1.0 O A:HOH1093 3.0 51.5 1.0 CG A:ASN263 3.1 44.2 1.0 OE2 A:GLU262 3.3 82.4 1.0 HD21 A:ASN263 3.3 65.5 1.0 CD A:GLU262 3.4 81.3 1.0 ND2 A:ASN263 3.5 54.6 1.0 HB3 A:ASP354 3.5 38.9 1.0 CG A:ASP354 3.6 55.7 1.0 HA A:ASN263 3.6 37.5 1.0 H A:ASP354 4.0 34.9 1.0 CB A:ASP354 4.1 32.4 1.0 HB A:THR352 4.1 36.6 1.0 O A:HOH1110 4.2 38.3 1.0 HB1 A:ALA148 4.3 45.4 1.0 CB A:ASN263 4.3 41.9 1.0 HG1 A:THR280 4.3 43.0 1.0 CA A:ASN263 4.3 31.2 1.0 HD22 A:ASN263 4.3 65.5 1.0 HG1 A:THR352 4.4 37.8 1.0 OD1 A:ASP354 4.6 69.2 1.0 O A:HOH987 4.7 44.3 1.0 N A:ASN263 4.7 29.5 1.0 HB2 A:ASP354 4.8 38.9 1.0 N A:ASP354 4.8 29.0 1.0 HB3 A:ASN263 4.8 50.4 1.0 HB2 A:ASN263 4.9 50.4 1.0 OG1 A:THR352 4.9 31.5 1.0 CB A:THR352 4.9 30.4 1.0 HG21 A:THR352 4.9 36.3 1.0 CG A:GLU262 4.9 47.9 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 AD012


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 AD012 within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg710 b:30.4 occ:1.00 O B:HOH1055 2.1 53.8 1.0 OE2 B:GLU262 2.3 45.5 1.0 O B:HOH804 2.3 41.5 1.0 O B:HOH917 2.4 47.4 1.0 OD2 B:ASP354 2.5 48.6 1.0 O B:HOH1050 2.7 44.3 1.0 OD1 B:ASP354 2.8 43.4 1.0 HG B:SER260 2.9 44.5 1.0 CG B:ASP354 3.0 48.4 1.0 CD B:GLU262 3.3 44.3 1.0 OG B:SER260 3.4 37.0 1.0 OE1 B:GLU262 3.9 31.2 1.0 O B:HOH942 4.1 42.0 1.0 O B:HOH955 4.2 44.9 1.0 O B:HOH1040 4.4 28.1 1.0 O B:HOH833 4.5 33.0 1.0 CB B:ASP354 4.5 33.5 1.0 HG3 B:GLU262 4.5 37.9 1.0 CG B:GLU262 4.5 31.5 1.0 O B:HOH840 4.5 46.9 1.0 O B:HOH1066 4.5 41.7 1.0 OD2 B:ASP255 4.5 30.5 1.0 HG2 B:GLU262 4.6 37.9 1.0 CB B:SER260 4.7 24.8 1.0 OD1 B:ASN263 4.7 43.4 1.0 HB2 B:ASP354 4.7 40.2 1.0 HB3 B:ASP354 4.8 40.2 1.0 HB2 B:SER260 4.9 29.8 1.0 HB3 B:SER260 5.0 29.8 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