Zinc 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
Magnesium	(Mg)	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 AD012 (pdb code 7q25). 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 AD012, PDB code: 7q25:
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 AD012


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 AD012 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn712 b:24.3 occ:1.00 NE2 A:HIS365 1.9 20.9 1.0 OE1 A:GLU389 2.0 21.8 1.0 O25 A:8J9701 2.1 23.3 1.0 NE2 A:HIS361 2.1 22.1 1.0 O24 A:8J9701 2.7 26.8 1.0 C23 A:8J9701 2.7 30.9 1.0 CE1 A:HIS365 2.9 21.9 1.0 CD A:GLU389 2.9 23.8 1.0 CD2 A:HIS365 3.0 23.3 1.0 HE1 A:HIS365 3.0 26.3 1.0 CE1 A:HIS361 3.0 26.6 1.0 CD2 A:HIS361 3.1 24.7 1.0 OE2 A:GLU389 3.1 23.5 1.0 HD2 A:HIS365 3.2 28.0 1.0 HE1 A:HIS361 3.2 32.0 1.0 HD2 A:HIS361 3.2 29.7 1.0 HE1 A:TYR501 3.3 25.1 1.0 HA A:GLU389 3.6 25.9 1.0 H051 A:8J9701 3.8 30.9 1.0 H241 A:1PE704 3.9 46.5 1.0 ND1 A:HIS365 4.0 24.2 1.0 CG A:HIS365 4.1 22.7 1.0 ND1 A:HIS361 4.1 22.3 1.0 C22 A:8J9701 4.1 24.9 1.0 CG A:HIS361 4.2 20.8 1.0 CE1 A:TYR501 4.2 20.9 1.0 CG A:GLU389 4.3 23.9 1.0 OH A:TYR501 4.4 23.1 1.0 H221 A:8J9701 4.4 29.9 1.0 HB3 A:GLU389 4.4 25.4 1.0 O A:HOH906 4.4 27.1 1.0 H271 A:8J9701 4.5 36.2 1.0 CA A:GLU389 4.5 21.5 1.0 O A:HOH1038 4.6 25.9 1.0 OE2 A:GLU362 4.6 25.2 1.0 CB A:GLU389 4.6 21.1 1.0 C05 A:8J9701 4.7 25.7 1.0 HG3 A:GLU389 4.7 28.7 1.0 H022 A:8J9701 4.7 34.5 1.0 C24 A:1PE704 4.7 38.7 1.0 H191 A:8J9701 4.7 32.5 1.0 H142 A:1PE704 4.7 45.8 1.0 HD1 A:HIS365 4.8 29.1 1.0 CZ A:TYR501 4.8 24.4 1.0 H141 A:1PE704 4.8 45.8 1.0 H071 A:8J9701 4.8 30.8 1.0 N21 A:8J9701 4.8 27.6 1.0 HG2 A:GLU389 4.9 28.7 1.0 HD1 A:HIS361 4.9 26.8 1.0 H262 A:8J9701 4.9 37.2 1.0 OE1 A:GLU362 4.9 23.9 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 AD012


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 AD012 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn708 b:24.2 occ:1.00 O24 B:8J9702 1.8 24.3 1.0 OE1 B:GLU389 1.9 22.8 1.0 NE2 B:HIS365 2.0 24.4 1.0 NE2 B:HIS361 2.0 23.8 1.0 O25 B:8J9702 2.4 29.8 1.0 C23 B:8J9702 2.6 21.8 1.0 CD B:GLU389 2.9 20.2 1.0 CE1 B:HIS361 2.9 22.2 1.0 CE1 B:HIS365 2.9 35.8 1.0 HE1 B:HIS361 3.0 26.7 1.0 CD2 B:HIS365 3.1 30.0 1.0 CD2 B:HIS361 3.1 25.2 1.0 HE1 B:HIS365 3.1 43.0 1.0 OE2 B:GLU389 3.2 29.0 1.0 HD2 B:HIS365 3.3 36.1 1.0 HE1 B:TYR501 3.3 26.7 1.0 HD2 B:HIS361 3.3 30.3 1.0 HA B:GLU389 3.7 29.2 1.0 H051 B:8J9702 3.8 34.9 1.0 C22 B:8J9702 4.0 25.7 1.0 ND1 B:HIS361 4.0 23.7 1.0 ND1 B:HIS365 4.1 31.1 1.0 CG B:HIS361 4.1 20.1 1.0 CG B:HIS365 4.2 28.3 1.0 CE1 B:TYR501 4.2 22.2 1.0 CG B:GLU389 4.3 27.9 1.0 H221 B:8J9702 4.3 30.9 1.0 O B:HOH983 4.4 29.8 1.0 OH B:TYR501 4.4 25.3 1.0 H42 B:PG4706 4.4 30.1 1.0 H41 B:PG4706 4.5 30.1 1.0 H271 B:8J9702 4.5 41.9 1.0 HB3 B:GLU389 4.5 34.9 1.0 OE2 B:GLU362 4.5 27.4 1.0 CA B:GLU389 4.6 24.3 1.0 O B:HOH940 4.6 30.0 1.0 C05 B:8J9702 4.6 29.1 1.0 HG3 B:GLU389 4.7 33.5 1.0 CB B:GLU389 4.7 29.1 1.0 H31 B:PG4706 4.7 49.1 1.0 H262 B:8J9702 4.7 31.7 1.0 N21 B:8J9702 4.8 24.9 1.0 H071 B:8J9702 4.8 26.6 1.0 CZ B:TYR501 4.8 23.9 1.0 HD1 B:HIS361 4.8 28.5 1.0 H022 B:8J9702 4.8 36.7 1.0 H191 B:8J9702 4.8 31.7 1.0 C4 B:PG4706 4.8 25.1 1.0 HD1 B:HIS365 4.8 37.4 1.0 HG2 B:GLU389 4.9 33.5 1.0 OE1 B:GLU362 4.9 26.6 1.0 C26 B:8J9702 4.9 26.4 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