Chlorine 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
Zinc	(Zn)	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 AD013 (pdb code 7q26). 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 AD013, PDB code: 7q26:
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 AD013


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 AD013 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl703 b:19.8 occ:1.00 HH A:TYR202 2.2 24.9 1.0 HE A:ARG500 2.3 25.9 1.0 HB3 A:ARG500 2.7 24.0 1.0 HH21 A:ARG500 2.8 28.5 1.0 HB2 A:PRO497 2.9 23.9 1.0 HB2 A:PRO385 3.0 27.4 1.0 OH A:TYR202 3.1 20.8 1.0 HG2 A:PRO385 3.1 32.2 1.0 HE2 A:TYR202 3.1 27.0 1.0 O A:HOH1053 3.1 20.6 1.0 H A:ARG500 3.1 23.5 1.0 HG22 A:ILE499 3.1 24.6 1.0 NE A:ARG500 3.1 21.6 1.0 HE3 A:TRP201 3.2 31.9 1.0 HZ3 A:TRP201 3.3 31.6 1.0 NH2 A:ARG500 3.5 23.8 1.0 CB A:ARG500 3.6 20.0 1.0 CB A:PRO385 3.6 22.8 1.0 HG23 A:ILE499 3.7 24.6 1.0 HB3 A:PRO385 3.7 27.4 1.0 CB A:PRO497 3.7 20.0 1.0 N A:ARG500 3.7 19.6 1.0 CE2 A:TYR202 3.8 22.5 1.0 HG2 A:ARG500 3.8 24.2 1.0 HB3 A:PRO497 3.8 23.9 1.0 CG A:PRO385 3.8 26.8 1.0 CZ A:ARG500 3.8 23.8 1.0 CG2 A:ILE499 3.8 20.5 1.0 CZ A:TYR202 3.8 20.2 1.0 CE3 A:TRP201 3.9 26.6 1.0 CZ3 A:TRP201 4.0 26.4 1.0 CG A:ARG500 4.0 20.2 1.0 HG2 A:PRO497 4.0 25.1 1.0 CA A:ARG500 4.1 19.4 1.0 HA A:ARG500 4.1 23.3 1.0 CD A:ARG500 4.2 21.4 1.0 HG21 A:ILE499 4.2 24.6 1.0 HH22 A:ARG500 4.3 28.5 1.0 HB2 A:ARG500 4.3 24.0 1.0 HG3 A:PRO385 4.4 32.2 1.0 H A:ILE499 4.4 23.9 1.0 CG A:PRO497 4.5 20.9 1.0 HD2 A:PRO385 4.5 31.0 1.0 C A:ILE499 4.7 19.3 1.0 N A:ILE499 4.7 20.0 1.0 HD3 A:ARG500 4.8 25.6 1.0 CD A:PRO385 4.8 25.8 1.0 HD2 A:ARG500 4.8 25.6 1.0 C A:PRO497 4.8 21.2 1.0 O A:HOH989 4.8 18.5 1.0 CA A:PRO497 4.9 19.8 1.0 HG3 A:ARG500 5.0 24.2 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 AD013


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 AD013 within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl706 b:26.0 occ:1.00 HE B:ARG500 2.4 29.6 1.0 HB3 B:ARG500 2.7 26.4 1.0 HH21 B:ARG500 2.8 33.4 1.0 HB2 B:PRO497 2.9 28.1 1.0 O B:HOH995 3.1 30.4 1.0 OH B:TYR202 3.1 28.7 1.0 H B:ARG500 3.1 25.6 1.0 HB2 B:PRO385 3.1 37.0 1.0 HG22 B:ILE499 3.1 30.2 1.0 HE1 B:TYR202 3.1 38.6 1.0 HE3 B:TRP201 3.2 46.8 1.0 NE B:ARG500 3.2 24.7 1.0 HG2 B:PRO385 3.2 40.9 1.0 HZ3 B:TRP201 3.3 44.9 1.0 NH2 B:ARG500 3.5 27.9 1.0 HG23 B:ILE499 3.6 30.2 1.0 CB B:ARG500 3.6 22.0 1.0 HH B:TYR202 3.7 34.5 1.0 HB3 B:PRO497 3.7 28.1 1.0 CB B:PRO497 3.7 23.4 1.0 N B:ARG500 3.7 21.4 1.0 CB B:PRO385 3.7 30.8 1.0 CG2 B:ILE499 3.8 25.2 1.0 CE1 B:TYR202 3.8 32.2 1.0 HB3 B:PRO385 3.8 37.0 1.0 CZ B:ARG500 3.8 27.3 1.0 CE3 B:TRP201 3.9 39.0 1.0 CZ B:TYR202 3.9 30.0 1.0 CG B:PRO385 3.9 34.1 1.0 CZ3 B:TRP201 3.9 37.4 1.0 HG2 B:ARG500 3.9 25.9 1.0 CA B:ARG500 4.1 22.7 1.0 HG2 B:PRO497 4.1 33.1 1.0 HA B:ARG500 4.1 27.2 1.0 CG B:ARG500 4.1 21.6 1.0 HG21 B:ILE499 4.2 30.2 1.0 CD B:ARG500 4.2 22.8 1.0 HH22 B:ARG500 4.3 33.4 1.0 HB2 B:ARG500 4.3 26.4 1.0 H B:ILE499 4.4 28.0 1.0 CG B:PRO497 4.5 27.6 1.0 HG3 B:PRO385 4.5 40.9 1.0 HD2 B:PRO385 4.6 43.8 1.0 N B:ILE499 4.7 23.4 1.0 C B:ILE499 4.7 21.9 1.0 O B:HOH974 4.7 26.4 1.0 HD2 B:ARG500 4.8 27.3 1.0 C B:PRO497 4.8 24.9 1.0 HD3 B:ARG500 4.9 27.3 1.0 CA B:PRO497 4.9 24.0 1.0 CD B:PRO385 4.9 36.5 1.0 HB3 B:TRP198 5.0 39.9 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