Zinc 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
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 AD011 (pdb code 7q24). 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 AD011, PDB code: 7q24:
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 AD011


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 AD011 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn709 b:21.7 occ:1.00 O26 A:8KC712 1.9 27.8 1.0 OE1 A:GLU389 2.0 28.0 1.0 NE2 A:HIS365 2.2 28.9 1.0 NE2 A:HIS361 2.3 28.6 1.0 C24 A:8KC712 2.6 28.6 1.0 O25 A:8KC712 2.6 24.0 1.0 CD A:GLU389 2.9 21.8 1.0 HE1 A:HIS365 2.9 31.3 1.0 CE1 A:HIS365 2.9 26.0 1.0 CD2 A:HIS361 3.0 22.0 1.0 HD2 A:HIS361 3.1 26.4 1.0 OE2 A:GLU389 3.1 23.4 1.0 HE1 A:TYR501 3.2 28.2 1.0 CE1 A:HIS361 3.3 28.7 1.0 CD2 A:HIS365 3.4 29.0 1.0 HE1 A:HIS361 3.6 34.5 1.0 HA A:GLU389 3.7 34.0 1.0 HD2 A:HIS365 3.7 34.9 1.0 H171 A:8KC712 3.7 41.7 1.0 H112 A:P6G707 3.8 40.6 1.0 C23 A:8KC712 4.0 27.5 1.0 ND1 A:HIS365 4.1 26.8 1.0 CE1 A:TYR501 4.1 23.5 1.0 CG A:HIS361 4.2 28.8 1.0 CG A:GLU389 4.3 24.1 1.0 H231 A:8KC712 4.3 33.1 1.0 OH A:TYR501 4.3 25.1 1.0 ND1 A:HIS361 4.3 26.1 1.0 CG A:HIS365 4.4 23.4 1.0 HB3 A:GLU389 4.4 32.6 1.0 O A:HOH898 4.4 25.6 1.0 H122 A:P6G707 4.5 46.4 1.0 O A:HOH946 4.5 28.8 1.0 CA A:GLU389 4.5 28.3 1.0 C17 A:8KC712 4.6 34.7 1.0 CB A:GLU389 4.6 27.1 1.0 OE2 A:GLU362 4.6 27.5 1.0 H201 A:8KC712 4.7 46.7 1.0 HG3 A:GLU389 4.7 29.0 1.0 CZ A:TYR501 4.7 22.2 1.0 C11 A:P6G707 4.7 33.8 1.0 N22 A:8KC712 4.8 31.4 1.0 H272 A:8KC712 4.8 35.6 1.0 HG2 A:GLU389 4.8 29.0 1.0 HD1 A:HIS365 4.8 32.3 1.0 H221 A:8KC712 4.8 37.7 1.0 OE1 A:GLU362 4.9 26.4 1.0 H151 A:8KC712 4.9 35.8 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 AD011


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 AD011 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn709 b:23.2 occ:1.00 OE1 B:GLU389 1.9 24.8 1.0 O25 B:8KC712 1.9 30.4 1.0 NE2 B:HIS365 2.2 31.9 1.0 NE2 B:HIS361 2.3 27.0 1.0 O26 B:8KC712 2.5 27.0 1.0 C24 B:8KC712 2.5 30.1 1.0 CD B:GLU389 2.8 29.6 1.0 CE1 B:HIS365 3.1 29.0 1.0 CD2 B:HIS361 3.1 23.2 1.0 OE2 B:GLU389 3.1 24.6 1.0 HE1 B:HIS365 3.2 34.9 1.0 HD2 B:HIS361 3.2 27.9 1.0 HE1 B:TYR501 3.2 36.7 1.0 CE1 B:HIS361 3.3 34.1 1.0 CD2 B:HIS365 3.3 30.5 1.0 HE1 B:HIS361 3.5 41.0 1.0 HD2 B:HIS365 3.5 36.6 1.0 HA B:GLU389 3.6 33.7 1.0 H171 B:8KC712 3.7 44.1 1.0 H42 B:PG4704 3.9 47.3 1.0 C23 B:8KC712 4.0 33.0 1.0 CE1 B:TYR501 4.1 30.5 1.0 H231 B:8KC712 4.2 39.6 1.0 CG B:GLU389 4.2 21.8 1.0 ND1 B:HIS365 4.2 31.8 1.0 CG B:HIS361 4.3 29.5 1.0 OH B:TYR501 4.3 29.5 1.0 ND1 B:HIS361 4.3 32.8 1.0 HB3 B:GLU389 4.3 33.3 1.0 O B:HOH868 4.3 31.3 1.0 CG B:HIS365 4.4 33.6 1.0 O B:HOH898 4.5 31.3 1.0 C17 B:8KC712 4.5 36.7 1.0 CA B:GLU389 4.5 28.0 1.0 CB B:GLU389 4.6 27.7 1.0 HG3 B:GLU389 4.6 25.8 1.0 OE2 B:GLU362 4.7 32.7 1.0 N22 B:8KC712 4.7 36.7 1.0 CZ B:TYR501 4.7 26.6 1.0 H221 B:8KC712 4.7 44.1 1.0 H272 B:8KC712 4.7 40.1 1.0 C4 B:PG4704 4.8 39.4 1.0 H151 B:8KC712 4.8 39.4 1.0 HG2 B:GLU389 4.8 25.8 1.0 H202 B:8KC712 4.8 52.1 1.0 OE1 B:GLU362 4.9 28.3 1.0 C27 B:8KC712 5.0 33.3 1.0 HD1 B:HIS365 5.0 38.2 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