Chlorine in PDB 7q28: Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain in Complex with Dual Ace/Nep Inhibitor AD012

All present enzymatic activity of Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain in Complex with Dual Ace/Nep Inhibitor AD012:
3.4.15.1;

The structure of Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain in Complex with Dual Ace/Nep Inhibitor AD012, PDB code: 7q28 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)	71.55 / 1.65
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	56.254, 84.78, 133.376, 90, 90, 90
R / Rfree (%)	16.3 / 18.3

The structure of Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain in Complex with Dual Ace/Nep Inhibitor AD012 also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Chlorine atom in the Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain in Complex with Dual Ace/Nep Inhibitor AD012 (pdb code 7q28). 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 C-Domain in Complex with Dual Ace/Nep Inhibitor AD012, PDB code: 7q28:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of Angiotensin-1 Converting Enzyme C-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 C-Domain in Complex with Dual Ace/Nep Inhibitor AD012 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl710 b:20.0 occ:1.00 HE A:ARG186 2.4 22.7 1.0 HE1 A:TRP485 2.5 19.0 1.0 HH21 A:ARG186 2.5 22.2 1.0 HH21 A:ARG489 2.7 21.3 1.0 HB3 A:ASP507 2.9 21.1 1.0 HZ2 A:TRP486 3.0 22.5 1.0 NE A:ARG186 3.2 18.9 1.0 NH2 A:ARG489 3.2 17.7 1.0 NE1 A:TRP485 3.3 15.8 1.0 NH2 A:ARG186 3.3 18.5 1.0 O A:HOH985 3.3 24.4 1.0 CZ2 A:TRP486 3.5 18.8 1.0 HE A:ARG489 3.5 24.1 1.0 HH22 A:ARG489 3.7 21.3 1.0 HZ2 A:TRP485 3.7 23.1 1.0 CZ A:ARG186 3.7 19.3 1.0 HZ2 A:TRP182 3.8 20.8 1.0 CB A:ASP507 3.8 17.6 1.0 HH2 A:TRP486 3.9 23.6 1.0 CZ A:ARG489 3.9 18.7 1.0 NE A:ARG489 3.9 20.1 1.0 HB2 A:ASP507 4.0 21.1 1.0 HH22 A:ARG186 4.0 22.2 1.0 CH2 A:TRP486 4.0 19.6 1.0 CE2 A:TRP485 4.1 16.4 1.0 CZ2 A:TRP485 4.3 19.2 1.0 HD3 A:ARG186 4.3 23.6 1.0 CD1 A:TRP485 4.3 15.5 1.0 CD A:ARG186 4.4 19.7 1.0 HD1 A:TRP279 4.4 21.5 1.0 CE2 A:TRP486 4.4 17.8 1.0 CZ2 A:TRP182 4.4 17.4 1.0 HD1 A:TRP485 4.4 18.6 1.0 O A:ASP507 4.5 16.6 1.0 CG A:ASP507 4.6 18.6 1.0 HE1 A:TRP182 4.6 22.0 1.0 HE1 A:TRP486 4.6 22.0 1.0 C A:ASP507 4.7 18.2 1.0 HG2 A:ARG186 4.7 22.9 1.0 O A:HOH1053 4.8 17.2 1.0 NE1 A:TRP486 4.8 18.3 1.0 CA A:ASP507 4.8 16.5 1.0 HA A:TRP279 4.9 17.2 1.0 OD2 A:ASP507 4.9 20.5 1.0 HG3 A:ARG489 4.9 18.9 1.0 HD3 A:ARG489 5.0 22.8 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of Angiotensin-1 Converting Enzyme C-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 C-Domain in Complex with Dual Ace/Nep Inhibitor AD012 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl711 b:29.1 occ:1.00 HE A:ARG522 2.5 22.4 1.0 HB3 A:ARG522 2.7 20.0 1.0 HB2 A:PRO519 2.8 22.6 1.0 OH A:TYR224 2.9 24.3 1.0 H A:ARG522 2.9 17.2 1.0 HE1 A:TYR224 3.0 22.7 1.0 HG22 A:ILE521 3.0 22.6 1.0 O A:HOH1019 3.0 28.9 1.0 HH21 A:ARG522 3.0 30.9 1.0 HB2 A:PRO407 3.2 21.8 1.0 HE3 A:MET223 3.3 30.1 0.7 NE A:ARG522 3.4 18.6 1.0 HH A:TYR224 3.4 29.1 1.0 HG2 A:PRO407 3.4 22.8 1.0 HB3 A:PRO519 3.5 22.6 1.0 CB A:ARG522 3.5 16.6 1.0 N A:ARG522 3.5 14.3 1.0 CB A:PRO519 3.6 18.8 1.0 CE1 A:TYR224 3.6 18.9 1.0 HE1 A:MET223 3.7 30.1 0.7 HG2 A:ARG522 3.7 19.9 1.0 CZ A:TYR224 3.7 17.6 1.0 HG23 A:ILE521 3.8 22.6 1.0 NH2 A:ARG522 3.8 25.8 1.0 CG2 A:ILE521 3.8 18.9 1.0 CB A:PRO407 3.8 18.1 1.0 HB3 A:PRO407 3.8 21.8 1.0 CE A:MET223 3.9 25.1 0.7 CA A:ARG522 3.9 16.1 1.0 HA A:ARG522 4.0 19.4 1.0 CG A:ARG522 4.0 16.5 1.0 CZ A:ARG522 4.0 22.3 1.0 CG A:PRO407 4.1 19.0 1.0 HG2 A:PRO519 4.2 20.9 1.0 HG21 A:ILE521 4.2 22.6 1.0 H A:ILE521 4.3 19.1 1.0 HB2 A:ARG522 4.3 20.0 1.0 CD A:ARG522 4.3 17.7 1.0 HE2 A:MET223 4.3 30.1 0.7 CG A:PRO519 4.5 17.4 1.0 HH22 A:ARG522 4.5 30.9 1.0 C A:ILE521 4.5 15.4 1.0 N A:ILE521 4.5 15.9 1.0 O A:HOH940 4.6 20.6 1.0 C A:PRO519 4.6 16.0 1.0 SD A:MET223 4.7 30.3 0.3 HG3 A:PRO407 4.7 22.8 1.0 CA A:PRO519 4.7 16.6 1.0 HD2 A:PRO407 4.8 21.5 1.0 N A:TYR520 4.8 14.8 1.0 H A:TYR520 4.9 17.8 1.0 CD1 A:TYR224 4.9 20.2 1.0 HB2 A:MET223 4.9 29.9 0.3 CA A:ILE521 4.9 14.0 1.0 HD2 A:ARG522 4.9 21.3 1.0 O A:PRO519 4.9 17.5 1.0 CB A:ILE521 4.9 16.8 1.0 HG3 A:ARG522 4.9 19.9 1.0 HD3 A:ARG522 5.0 21.3 1.0 HB2 A:MET223 5.0 30.3 0.7 CE2 A:TYR224 5.0 19.4 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