Zinc 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:

Magnesium	(Mg)	2 atoms
Chlorine	(Cl)	2 atoms

The binding sites of Zinc 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 Zinc atom.
In total 2 binding sites of Zinc 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 Zinc binding site number: 1; 2;

Zinc 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 Zinc with other atoms in the Zn 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:Zn702 b:21.8 occ:1.00 NE2 A:HIS365 1.9 21.8 1.0 OE1 A:GLU389 2.0 23.6 1.0 O31 A:8JV701 2.0 22.9 1.0 NE2 A:HIS361 2.1 23.1 1.0 O01 A:8JV701 2.6 24.5 1.0 C02 A:8JV701 2.6 27.1 1.0 CE1 A:HIS365 2.8 24.4 1.0 CD A:GLU389 2.9 22.3 1.0 HE1 A:HIS365 2.9 29.3 1.0 CD2 A:HIS365 3.0 23.1 1.0 CE1 A:HIS361 3.0 21.5 1.0 CD2 A:HIS361 3.1 24.1 1.0 OE2 A:GLU389 3.1 24.4 1.0 HE1 A:HIS361 3.2 25.8 1.0 HE1 A:TYR501 3.2 24.0 1.0 HD2 A:HIS365 3.2 27.8 1.0 HD2 A:HIS361 3.3 28.9 1.0 HA A:GLU389 3.6 29.8 1.0 H241 A:1PE707 3.8 36.7 1.0 H051 A:8JV701 3.8 30.1 1.0 ND1 A:HIS365 3.9 23.5 1.0 CG A:HIS365 4.1 22.0 1.0 ND1 A:HIS361 4.1 21.1 1.0 C03 A:8JV701 4.1 26.1 1.0 CE1 A:TYR501 4.1 20.0 1.0 CG A:HIS361 4.2 19.7 1.0 H141 A:8JV701 4.2 31.6 1.0 CG A:GLU389 4.2 21.1 1.0 H242 A:8JV701 4.3 32.8 1.0 H031 A:8JV701 4.3 31.4 1.0 OH A:TYR501 4.4 21.4 1.0 HB3 A:GLU389 4.4 28.0 1.0 O A:HOH943 4.4 23.1 1.0 O A:HOH836 4.5 24.0 1.0 CA A:GLU389 4.5 24.9 1.0 H142 A:1PE707 4.6 35.5 1.0 CB A:GLU389 4.6 23.3 1.0 OE2 A:GLU362 4.6 24.1 1.0 C24 A:1PE707 4.6 30.6 1.0 HD1 A:HIS365 4.7 28.1 1.0 C05 A:8JV701 4.7 25.1 1.0 HG3 A:GLU389 4.7 25.3 1.0 CZ A:TYR501 4.8 21.0 1.0 H141 A:1PE707 4.8 35.5 1.0 HG2 A:GLU389 4.8 25.3 1.0 N04 A:8JV701 4.8 25.1 1.0 H1 A:8JV701 4.8 30.1 1.0 HD1 A:HIS361 4.9 25.3 1.0 C14 A:1PE707 4.9 29.6 1.0 OE1 A:GLU362 4.9 24.3 1.0 C23 A:8JV701 5.0 26.7 1.0

Zinc 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 Zinc with other atoms in the Zn 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:Zn705 b:20.1 occ:1.00 OE1 B:GLU389 1.8 20.8 1.0 NE2 B:HIS365 2.0 22.1 1.0 NE2 B:HIS361 2.0 21.0 1.0 O31 B:8JV701 2.0 23.5 1.0 O01 B:8JV701 2.3 26.1 1.0 C02 B:8JV701 2.5 23.5 1.0 CD B:GLU389 2.8 24.4 1.0 CE1 B:HIS365 2.8 26.1 1.0 CE1 B:HIS361 2.9 23.3 1.0 HE1 B:HIS365 3.0 31.3 1.0 HE1 B:HIS361 3.0 28.0 1.0 CD2 B:HIS361 3.0 22.7 1.0 OE2 B:GLU389 3.1 26.6 1.0 CD2 B:HIS365 3.1 22.9 1.0 HE1 B:TYR501 3.2 26.5 1.0 HD2 B:HIS361 3.3 27.3 1.0 HD2 B:HIS365 3.4 27.6 1.0 HA B:GLU389 3.6 30.9 1.0 H051 B:8JV701 3.8 30.8 1.0 H41 B:PG4708 3.8 39.8 1.0 ND1 B:HIS361 4.0 24.4 1.0 ND1 B:HIS365 4.0 25.2 1.0 C03 B:8JV701 4.0 24.4 1.0 CG B:HIS361 4.1 20.6 1.0 CE1 B:TYR501 4.1 22.1 1.0 CG B:GLU389 4.1 24.2 1.0 CG B:HIS365 4.2 25.0 1.0 H141 B:8JV701 4.2 30.5 1.0 HB3 B:GLU389 4.3 31.2 1.0 OH B:TYR501 4.3 22.6 1.0 H031 B:8JV701 4.3 29.3 1.0 H242 B:8JV701 4.4 34.6 1.0 O B:HOH972 4.4 25.3 1.0 CA B:GLU389 4.5 25.8 1.0 H42 B:PG4708 4.5 39.8 1.0 O B:HOH986 4.5 27.1 1.0 CB B:GLU389 4.5 26.0 1.0 HG3 B:GLU389 4.6 29.1 1.0 C4 B:PG4708 4.6 33.1 1.0 OE2 B:GLU362 4.6 24.6 1.0 C05 B:8JV701 4.6 25.7 1.0 HG2 B:GLU389 4.7 29.1 1.0 CZ B:TYR501 4.7 21.6 1.0 HD1 B:HIS361 4.7 29.3 1.0 N04 B:8JV701 4.8 25.2 1.0 H1 B:8JV701 4.8 30.2 1.0 HD1 B:HIS365 4.8 30.2 1.0 H232 B:8JV701 4.8 30.1 1.0 C23 B:8JV701 4.9 25.1 1.0 OE1 B:GLU362 5.0 24.7 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