Chlorine in PDB 7q27: Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain in Complex with Dual Ace/Nep Inhibitor AD011

All present enzymatic activity of Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain in Complex with Dual Ace/Nep Inhibitor AD011:
3.4.15.1;

The structure of Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain in Complex with Dual Ace/Nep Inhibitor AD011, PDB code: 7q27 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)	47.13 / 1.50
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	56.454, 85.586, 134.052, 90, 90, 90
R / Rfree (%)	14.9 / 17.8

The structure of Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain in Complex with Dual Ace/Nep Inhibitor AD011 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 AD011 (pdb code 7q27). 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 AD011, PDB code: 7q27:
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 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 C-Domain in Complex with Dual Ace/Nep Inhibitor AD011 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl708 b:12.9 occ:1.00 HE A:ARG186 2.4 11.0 1.0 HH21 A:ARG186 2.5 12.0 1.0 HE1 A:TRP485 2.5 12.3 1.0 HH21 A:ARG489 2.8 13.2 1.0 HB3 A:ASP507 2.9 10.9 1.0 HZ2 A:TRP486 3.1 12.0 1.0 NE A:ARG186 3.2 9.2 1.0 NH2 A:ARG186 3.2 10.0 1.0 NH2 A:ARG489 3.3 11.0 1.0 O A:HOH1042 3.3 16.9 1.0 NE1 A:TRP485 3.3 10.2 1.0 CZ2 A:TRP486 3.6 10.0 1.0 HE A:ARG489 3.6 10.7 1.0 HH22 A:ARG489 3.7 13.2 1.0 CZ A:ARG186 3.7 10.0 1.0 HZ2 A:TRP182 3.8 8.6 1.0 CB A:ASP507 3.8 9.1 1.0 HZ2 A:TRP485 3.9 11.9 1.0 CZ A:ARG489 3.9 9.6 1.0 NE A:ARG489 3.9 8.9 1.0 HH22 A:ARG186 4.0 12.0 1.0 HB2 A:ASP507 4.0 10.9 1.0 HH2 A:TRP486 4.0 11.8 1.0 CH2 A:TRP486 4.1 9.9 1.0 CE2 A:TRP485 4.2 8.9 1.0 HD3 A:ARG186 4.2 14.2 1.0 CD A:ARG186 4.3 11.9 1.0 CD1 A:TRP485 4.3 10.1 1.0 HD1 A:TRP279 4.3 12.8 1.0 CE2 A:TRP486 4.4 8.3 1.0 CZ2 A:TRP485 4.4 9.9 1.0 HD1 A:TRP485 4.4 12.1 1.0 CZ2 A:TRP182 4.5 7.2 1.0 O A:ASP507 4.5 10.9 1.0 HE1 A:TRP486 4.5 10.8 1.0 CG A:ASP507 4.6 10.1 1.0 HE1 A:TRP182 4.6 10.5 1.0 HG2 A:ARG186 4.7 11.3 1.0 C A:ASP507 4.7 9.2 1.0 NE1 A:TRP486 4.8 9.0 1.0 O A:HOH1141 4.8 10.4 1.0 HD3 A:ARG489 4.8 11.6 1.0 HA A:TRP279 4.8 7.6 1.0 CA A:ASP507 4.8 7.9 1.0 HG3 A:ARG489 4.9 11.6 1.0 OD2 A:ASP507 5.0 10.6 1.0 CD A:ARG489 5.0 9.7 1.0 NH1 A:ARG489 5.0 9.6 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 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 C-Domain in Complex with Dual Ace/Nep Inhibitor AD011 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl709 b:11.5 occ:1.00 HH A:TYR224 2.2 13.8 1.0 HE A:ARG522 2.3 11.0 1.0 HB3 A:ARG522 2.7 9.5 1.0 HH21 A:ARG522 2.8 14.1 1.0 HB2 A:PRO519 2.8 8.6 1.0 H A:ARG522 2.8 7.6 1.0 HG22 A:ILE521 3.0 11.2 1.0 HE1 A:TYR224 3.0 9.3 1.0 HB2 A:PRO407 3.1 12.9 1.0 OH A:TYR224 3.1 11.5 1.0 O A:HOH1212 3.1 13.4 1.0 NE A:ARG522 3.2 9.2 1.0 HG2 A:PRO407 3.4 12.1 1.0 HE3 A:MET223 3.5 17.2 1.0 N A:ARG522 3.5 6.4 1.0 CB A:ARG522 3.5 7.9 1.0 NH2 A:ARG522 3.6 11.7 1.0 HB3 A:PRO519 3.6 8.6 1.0 CB A:PRO519 3.6 7.2 1.0 HG23 A:ILE521 3.6 11.2 1.0 CE1 A:TYR224 3.7 7.8 1.0 CB A:PRO407 3.7 10.8 1.0 HG2 A:ARG522 3.7 9.3 1.0 HE1 A:MET223 3.7 17.2 1.0 CG2 A:ILE521 3.7 9.4 1.0 HB3 A:PRO407 3.8 12.9 1.0 CZ A:TYR224 3.8 8.3 1.0 CZ A:ARG522 3.8 11.5 1.0 CA A:ARG522 3.9 7.7 1.0 CG A:ARG522 4.0 7.8 1.0 HA A:ARG522 4.0 9.2 1.0 CG A:PRO407 4.0 10.0 1.0 CE A:MET223 4.0 14.3 1.0 H A:ILE521 4.1 7.7 1.0 CD A:ARG522 4.2 10.3 1.0 HG2 A:PRO519 4.2 9.9 1.0 HG21 A:ILE521 4.2 11.2 1.0 HB2 A:ARG522 4.3 9.5 1.0 HH22 A:ARG522 4.3 14.1 1.0 N A:ILE521 4.4 6.4 1.0 C A:ILE521 4.5 5.7 1.0 CG A:PRO519 4.5 8.3 1.0 HE2 A:MET223 4.5 17.2 1.0 C A:PRO519 4.6 7.4 1.0 HG3 A:PRO407 4.6 12.1 1.0 CA A:PRO519 4.7 6.4 1.0 HD2 A:PRO407 4.7 11.5 1.0 HD2 A:ARG522 4.8 12.4 1.0 O A:HOH1001 4.8 12.0 1.0 HD3 A:ARG522 4.8 12.4 1.0 O A:PRO519 4.8 8.5 1.0 CA A:ILE521 4.8 7.1 1.0 N A:TYR520 4.8 8.4 1.0 CB A:ILE521 4.9 7.7 1.0 CD1 A:TYR224 4.9 10.7 1.0 HG3 A:ARG522 4.9 9.3 1.0 H A:TYR520 4.9 10.0 1.0 HB2 A:MET223 5.0 14.1 1.0 CD A:PRO407 5.0 9.6 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