Chlorine 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:

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


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 AD011 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl710 b:24.9 occ:1.00 HH A:TYR202 2.3 31.0 1.0 HE A:ARG500 2.4 27.1 1.0 HB3 A:ARG500 2.7 29.1 1.0 HH21 A:ARG500 2.8 33.5 1.0 HB2 A:PRO497 2.9 27.3 1.0 HG2 A:PRO385 3.1 34.9 1.0 O A:HOH985 3.1 27.6 1.0 HB2 A:PRO385 3.1 31.2 1.0 HE2 A:TYR202 3.1 32.8 1.0 OH A:TYR202 3.1 25.8 1.0 HG22 A:ILE499 3.2 25.5 1.0 H A:ARG500 3.2 26.7 1.0 NE A:ARG500 3.2 22.6 1.0 HE3 A:TRP201 3.3 40.1 1.0 HZ3 A:TRP201 3.4 37.4 1.0 NH2 A:ARG500 3.5 27.8 1.0 HB3 A:PRO497 3.6 27.3 1.0 CB A:ARG500 3.6 24.2 1.0 CB A:PRO497 3.6 22.7 1.0 CB A:PRO385 3.7 25.9 1.0 HG23 A:ILE499 3.7 25.5 1.0 CE2 A:TYR202 3.8 27.2 1.0 CG A:PRO385 3.8 29.1 1.0 N A:ARG500 3.8 22.2 1.0 HB3 A:PRO385 3.8 31.2 1.0 CZ A:ARG500 3.9 30.1 1.0 CG2 A:ILE499 3.9 21.2 1.0 CZ A:TYR202 3.9 24.7 1.0 HG2 A:ARG500 3.9 25.1 1.0 CE3 A:TRP201 4.0 33.4 1.0 CZ3 A:TRP201 4.0 31.1 1.0 HG2 A:PRO497 4.1 27.7 1.0 CA A:ARG500 4.1 21.9 1.0 CG A:ARG500 4.1 20.8 1.0 HA A:ARG500 4.2 26.3 1.0 HG21 A:ILE499 4.3 25.5 1.0 HH22 A:ARG500 4.3 33.5 1.0 CD A:ARG500 4.3 25.1 1.0 HB2 A:ARG500 4.3 29.1 1.0 HG3 A:PRO385 4.4 34.9 1.0 CG A:PRO497 4.5 23.0 1.0 HD2 A:PRO385 4.5 31.2 1.0 H A:ILE499 4.5 26.3 1.0 CD A:PRO385 4.8 25.9 1.0 C A:PRO497 4.8 22.4 1.0 C A:ILE499 4.8 19.2 1.0 N A:ILE499 4.8 21.9 1.0 CA A:PRO497 4.8 23.4 1.0 HD3 A:ARG500 4.9 30.2 1.0 HD2 A:ARG500 4.9 30.2 1.0 O A:HOH912 4.9 23.0 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 AD011


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 AD011 within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl710 b:33.3 occ:1.00 HH B:TYR202 2.3 38.9 1.0 HE B:ARG500 2.5 34.2 1.0 HB3 B:ARG500 2.7 35.2 1.0 HB2 B:PRO497 2.9 35.8 1.0 HH21 B:ARG500 2.9 38.9 1.0 HE2 B:TYR202 3.0 40.0 1.0 HB2 B:PRO385 3.1 39.1 1.0 O B:HOH933 3.1 33.5 1.0 OH B:TYR202 3.1 32.4 1.0 HG22 B:ILE499 3.2 32.6 1.0 H B:ARG500 3.2 28.3 1.0 HG2 B:PRO385 3.2 38.2 1.0 HE3 B:TRP201 3.3 56.3 1.0 NE B:ARG500 3.3 28.4 1.0 HG23 B:ILE499 3.5 32.6 1.0 HZ3 B:TRP201 3.6 53.6 1.0 CB B:ARG500 3.6 29.2 1.0 NH2 B:ARG500 3.7 32.3 1.0 CB B:PRO385 3.7 32.5 1.0 CE2 B:TYR202 3.7 33.3 1.0 HB3 B:PRO497 3.7 35.8 1.0 CB B:PRO497 3.7 29.8 1.0 HB3 B:PRO385 3.8 39.1 1.0 CG2 B:ILE499 3.8 27.1 1.0 N B:ARG500 3.8 23.5 1.0 HG2 B:ARG500 3.8 31.7 1.0 CZ B:TYR202 3.9 32.8 1.0 CG B:PRO385 3.9 31.8 1.0 CZ B:ARG500 4.0 33.5 1.0 CE3 B:TRP201 4.0 46.8 1.0 CA B:ARG500 4.1 26.1 1.0 CG B:ARG500 4.1 26.4 1.0 HG2 B:PRO497 4.1 37.3 1.0 HA B:ARG500 4.1 31.3 1.0 HG21 B:ILE499 4.2 32.6 1.0 CZ3 B:TRP201 4.2 44.6 1.0 CD B:ARG500 4.3 31.9 1.0 HB2 B:ARG500 4.3 35.2 1.0 HH22 B:ARG500 4.4 38.9 1.0 HG3 B:PRO385 4.5 38.2 1.0 H B:ILE499 4.5 25.6 1.0 CG B:PRO497 4.5 31.0 1.0 HD2 B:PRO385 4.6 42.0 1.0 C B:ILE499 4.8 30.5 1.0 N B:ILE499 4.8 21.2 1.0 C B:PRO497 4.8 35.0 1.0 O B:HOH832 4.9 27.6 1.0 CD B:PRO385 4.9 35.0 1.0 HD3 B:ARG500 4.9 38.4 1.0 CA B:PRO497 4.9 27.7 1.0 HD2 B:ARG500 4.9 38.4 1.0 CD2 B:TYR202 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