Chlorine 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:

Zinc	(Zn)	2 atoms
Magnesium	(Mg)	2 atoms

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

Chlorine 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 Chlorine with other atoms in the Cl 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:Cl713 b:22.6 occ:1.00 HH A:TYR202 2.2 26.4 1.0 HE A:ARG500 2.4 26.7 1.0 HB3 A:ARG500 2.7 23.6 1.0 HH21 A:ARG500 2.9 28.4 1.0 HB2 A:PRO497 2.9 21.9 1.0 OH A:TYR202 3.0 21.9 1.0 HG2 A:PRO385 3.0 29.2 1.0 O A:HOH1075 3.1 23.5 1.0 HE2 A:TYR202 3.1 26.3 1.0 H A:ARG500 3.1 22.8 1.0 HB2 A:PRO385 3.1 27.5 1.0 HG22 A:ILE499 3.2 23.1 1.0 NE A:ARG500 3.2 22.2 1.0 HE3 A:TRP201 3.3 30.9 1.0 HZ3 A:TRP201 3.3 32.8 1.0 CB A:ARG500 3.6 19.6 1.0 NH2 A:ARG500 3.6 23.6 1.0 CB A:PRO497 3.7 18.2 1.0 N A:ARG500 3.7 19.0 1.0 CB A:PRO385 3.7 22.9 1.0 CE2 A:TYR202 3.8 21.9 1.0 HG23 A:ILE499 3.8 23.1 1.0 HB3 A:PRO497 3.8 21.9 1.0 CG A:PRO385 3.8 24.3 1.0 HG2 A:ARG500 3.8 22.1 1.0 CZ A:TYR202 3.8 19.9 1.0 CZ A:ARG500 3.9 26.5 1.0 CG2 A:ILE499 3.9 19.3 1.0 HB3 A:PRO385 3.9 27.5 1.0 CE3 A:TRP201 3.9 25.7 1.0 CZ3 A:TRP201 3.9 27.3 1.0 HG2 A:PRO497 4.0 25.0 1.0 CA A:ARG500 4.1 19.2 1.0 CG A:ARG500 4.1 18.4 1.0 HA A:ARG500 4.1 23.1 1.0 CD A:ARG500 4.2 20.0 1.0 HB2 A:ARG500 4.3 23.6 1.0 HG21 A:ILE499 4.3 23.1 1.0 HH22 A:ARG500 4.3 28.4 1.0 H A:ILE499 4.4 23.9 1.0 HG3 A:PRO385 4.4 29.2 1.0 CG A:PRO497 4.5 20.8 1.0 HD2 A:PRO385 4.5 27.6 1.0 N A:ILE499 4.7 19.9 1.0 C A:ILE499 4.7 20.9 1.0 C A:PRO497 4.8 22.6 1.0 CD A:PRO385 4.8 22.9 1.0 HD2 A:ARG500 4.8 24.1 1.0 HD3 A:ARG500 4.8 24.1 1.0 CA A:PRO497 4.9 20.2 1.0 O A:HOH1019 4.9 20.9 1.0 N A:TYR498 5.0 19.4 1.0 H A:TYR498 5.0 23.4 1.0

Chlorine 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 Chlorine with other atoms in the Cl 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:Cl709 b:29.4 occ:1.00 HE B:ARG500 2.4 35.3 1.0 HB3 B:ARG500 2.7 28.9 1.0 HB2 B:PRO497 2.8 33.6 1.0 HH21 B:ARG500 2.8 35.1 1.0 H B:ARG500 3.1 26.3 1.0 O B:HOH995 3.1 33.4 1.0 OH B:TYR202 3.1 30.6 1.0 HB2 B:PRO385 3.1 39.6 1.0 HZ3 B:TRP201 3.1 52.5 1.0 HG22 B:ILE499 3.1 32.1 1.0 HE3 B:TRP201 3.1 50.6 1.0 HE2 B:TYR202 3.2 42.9 1.0 NE B:ARG500 3.2 29.4 1.0 HG2 B:PRO385 3.2 43.1 1.0 HH B:TYR202 3.5 36.8 1.0 NH2 B:ARG500 3.6 29.2 1.0 CB B:ARG500 3.6 24.1 1.0 CB B:PRO497 3.6 28.0 1.0 HB3 B:PRO497 3.7 33.6 1.0 N B:ARG500 3.7 21.9 1.0 CB B:PRO385 3.7 32.9 1.0 CE3 B:TRP201 3.8 42.1 1.0 CZ3 B:TRP201 3.8 43.7 1.0 HG23 B:ILE499 3.8 32.1 1.0 CE2 B:TYR202 3.8 35.7 1.0 HB3 B:PRO385 3.8 39.6 1.0 HG2 B:ARG500 3.8 28.1 1.0 CZ B:ARG500 3.9 27.8 1.0 CZ B:TYR202 3.9 31.2 1.0 CG2 B:ILE499 3.9 26.7 1.0 CG B:PRO385 3.9 35.9 1.0 HG2 B:PRO497 4.0 42.4 1.0 CG B:ARG500 4.1 23.4 1.0 CA B:ARG500 4.1 23.4 1.0 HA B:ARG500 4.1 28.2 1.0 CD B:ARG500 4.2 27.2 1.0 HB2 B:ARG500 4.3 28.9 1.0 HG21 B:ILE499 4.3 32.1 1.0 HH22 B:ARG500 4.3 35.1 1.0 H B:ILE499 4.4 29.6 1.0 CG B:PRO497 4.4 35.3 1.0 HG3 B:PRO385 4.6 43.1 1.0 HD2 B:PRO385 4.6 47.3 1.0 N B:ILE499 4.7 24.6 1.0 C B:ILE499 4.7 27.6 1.0 C B:PRO497 4.8 28.1 1.0 HD2 B:ARG500 4.8 32.7 1.0 O B:HOH933 4.8 28.2 1.0 CA B:PRO497 4.8 25.3 1.0 HD3 B:ARG500 4.8 32.7 1.0 CD B:PRO385 4.9 39.4 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