Magnesium in PDB 7q24: Crystal Structure of Angiotensin-1 Converting Enzyme N-Domain in Complex with Dual Ace/Nep Inhibitor AD011

All present enzymatic activity of Crystal Structure of Angiotensin-1 Converting Enzyme N-Domain in Complex with Dual Ace/Nep Inhibitor AD011:
3.4.15.1;

The structure of Crystal Structure of Angiotensin-1 Converting Enzyme N-Domain in Complex with Dual Ace/Nep Inhibitor AD011, PDB code: 7q24 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)	63.12 / 2.00
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	72.766, 77.608, 81.647, 88.93, 64.55, 75.01
R / Rfree (%)	18.5 / 21.4

The structure of Crystal Structure of Angiotensin-1 Converting Enzyme N-Domain in Complex with Dual Ace/Nep Inhibitor AD011 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 AD011 (pdb code 7q24). 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 AD011, PDB code: 7q24:
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 AD011


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 AD011 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg711 b:52.9 occ:1.00 OD1 A:ASN263 2.3 43.7 1.0 O A:HOH936 2.4 45.9 1.0 O A:HOH1022 2.5 43.6 1.0 OE2 A:GLU262 2.8 56.2 1.0 OD1 A:ASP354 2.9 51.5 1.0 OE1 A:GLU262 2.9 56.5 1.0 CD A:GLU262 3.3 56.3 1.0 CG A:ASN263 3.3 35.1 1.0 HD22 A:ASN263 3.6 46.2 1.0 CG A:ASP354 3.6 45.6 1.0 HB3 A:ASP354 3.8 47.5 1.0 ND2 A:ASN263 3.8 38.5 1.0 HB A:THR352 3.8 46.1 1.0 HA A:ASN263 3.9 41.4 1.0 H A:ASP354 4.0 39.6 1.0 HG1 A:THR280 4.1 42.0 1.0 CB A:ASP354 4.3 39.5 1.0 HG1 A:THR352 4.3 48.0 1.0 HB1 A:ALA148 4.4 54.2 1.0 OD2 A:ASP354 4.4 60.1 1.0 CB A:ASN263 4.5 39.7 1.0 CA A:ASN263 4.6 34.4 1.0 HG21 A:THR352 4.6 45.0 1.0 HD21 A:ASN263 4.6 46.2 1.0 CB A:THR352 4.7 38.4 1.0 CG A:GLU262 4.8 47.4 1.0 OG1 A:THR352 4.8 39.9 1.0 N A:ASP354 4.8 33.0 1.0 OG1 A:THR280 4.9 35.0 1.0 HB3 A:ASN263 4.9 47.8 1.0 HB2 A:ASP354 5.0 47.5 1.0 N A:ASN263 5.0 30.4 1.0 H A:MET353 5.0 42.8 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 AD011


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 AD011 within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg711 b:51.5 occ:1.00 O B:HOH854 2.4 54.7 1.0 OE2 B:GLU262 2.7 57.6 1.0 HG B:SER260 2.8 59.6 1.0 HB2 B:ASP354 3.3 50.7 1.0 O B:HOH925 3.4 50.4 1.0 OG B:SER260 3.4 49.6 1.0 OD2 B:ASP354 3.6 57.8 1.0 CD B:GLU262 3.7 59.9 1.0 H131 B:8KC712 3.8 62.4 1.0 O B:HOH1003 4.0 46.4 1.0 CB B:ASP354 4.1 42.2 1.0 C13 B:8KC712 4.3 52.0 1.0 CG B:ASP354 4.3 49.1 1.0 OE1 B:GLU262 4.3 51.6 1.0 HB3 B:ASP354 4.4 50.7 1.0 HD21 B:ASN263 4.5 54.6 1.0 H121 B:8KC712 4.5 52.6 1.0 HG3 B:GLU262 4.5 55.4 1.0 CB B:SER260 4.6 34.2 1.0 C12 B:8KC712 4.6 43.8 1.0 CG B:GLU262 4.7 46.1 1.0 HE21 B:GLN259 4.7 60.2 1.0 HB2 B:SER260 4.8 41.1 1.0 HB3 B:SER260 4.8 41.1 1.0 OD1 B:ASP255 4.8 40.5 1.0 HG2 B:GLU262 4.9 55.4 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