Chlorine in PDB 7q29: Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain in Complex with Dual Ace/Nep Inhibitor AD013

All present enzymatic activity of Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain in Complex with Dual Ace/Nep Inhibitor AD013:
3.4.15.1;

The structure of Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain in Complex with Dual Ace/Nep Inhibitor AD013, PDB code: 7q29 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)	66.36 / 1.60
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	56.164, 84.765, 132.728, 90, 90, 90
R / Rfree (%)	16.1 / 18.4

The structure of Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain in Complex with Dual Ace/Nep Inhibitor AD013 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 AD013 (pdb code 7q29). 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 AD013, PDB code: 7q29:
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 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 C-Domain in Complex with Dual Ace/Nep Inhibitor AD013 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl714 b:12.1 occ:1.00 HE A:ARG186 2.4 14.2 1.0 HE1 A:TRP485 2.4 13.8 1.0 HH21 A:ARG186 2.5 13.1 1.0 HH21 A:ARG489 2.6 15.5 1.0 HB3 A:ASP507 2.9 12.1 1.0 HZ2 A:TRP486 3.1 15.1 1.0 NE A:ARG186 3.2 11.8 1.0 NH2 A:ARG489 3.2 12.9 1.0 NH2 A:ARG186 3.2 11.0 1.0 NE1 A:TRP485 3.3 11.5 1.0 O A:HOH1061 3.3 16.2 1.0 HE A:ARG489 3.4 15.5 1.0 CZ2 A:TRP486 3.6 12.6 1.0 HH22 A:ARG489 3.7 15.5 1.0 CZ A:ARG186 3.7 11.4 1.0 HZ2 A:TRP485 3.7 13.2 1.0 CB A:ASP507 3.8 10.1 1.0 HZ2 A:TRP182 3.8 13.8 1.0 NE A:ARG489 3.8 12.9 1.0 CZ A:ARG489 3.9 10.9 1.0 HB2 A:ASP507 3.9 12.1 1.0 HH22 A:ARG186 4.0 13.1 1.0 HH2 A:TRP486 4.0 16.2 1.0 CH2 A:TRP486 4.1 13.5 1.0 CE2 A:TRP485 4.1 10.5 1.0 HD3 A:ARG186 4.2 13.7 1.0 CZ2 A:TRP485 4.3 11.0 1.0 CD1 A:TRP485 4.3 10.3 1.0 HD1 A:TRP279 4.3 10.9 1.0 CD A:ARG186 4.3 11.4 1.0 CE2 A:TRP486 4.4 11.3 1.0 HD1 A:TRP485 4.4 12.3 1.0 CZ2 A:TRP182 4.4 11.5 1.0 O A:ASP507 4.5 11.0 1.0 CG A:ASP507 4.6 12.7 1.0 HE1 A:TRP486 4.6 17.2 1.0 HE1 A:TRP182 4.7 13.2 1.0 HG2 A:ARG186 4.7 14.4 1.0 C A:ASP507 4.7 10.6 1.0 NE1 A:TRP486 4.8 14.3 1.0 CA A:ASP507 4.8 11.3 1.0 O A:HOH1070 4.8 11.4 1.0 HA A:TRP279 4.8 9.9 1.0 HG3 A:ARG489 4.9 11.6 1.0 OD2 A:ASP507 4.9 12.5 1.0 HD3 A:ARG489 4.9 13.7 1.0 NH1 A:ARG489 5.0 9.7 1.0 CD A:ARG489 5.0 11.4 1.0 HD2 A:ARG186 5.0 13.7 1.0 NH1 A:ARG186 5.0 11.0 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 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 C-Domain in Complex with Dual Ace/Nep Inhibitor AD013 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl715 b:11.5 occ:1.00 HH A:TYR224 2.2 15.4 1.0 HE A:ARG522 2.3 10.7 1.0 HB3 A:ARG522 2.7 11.6 1.0 HH21 A:ARG522 2.8 15.1 1.0 HB2 A:PRO519 2.8 10.6 1.0 H A:ARG522 2.9 8.6 1.0 HG22 A:ILE521 3.0 10.3 1.0 HE1 A:TYR224 3.0 13.6 1.0 OH A:TYR224 3.1 12.8 1.0 HB2 A:PRO407 3.1 13.7 1.0 O A:HOH1029 3.1 12.9 1.0 NE A:ARG522 3.2 8.9 1.0 HG2 A:PRO407 3.3 15.8 1.0 HE1 A:MET223 3.5 17.2 1.0 HE3 A:MET223 3.5 17.2 1.0 CB A:ARG522 3.5 9.7 1.0 N A:ARG522 3.5 7.2 1.0 NH2 A:ARG522 3.5 12.6 1.0 HB3 A:PRO519 3.6 10.6 1.0 CB A:PRO519 3.6 8.8 1.0 HG23 A:ILE521 3.7 10.3 1.0 CB A:PRO407 3.7 11.4 1.0 CE1 A:TYR224 3.7 11.4 1.0 HG2 A:ARG522 3.7 12.9 1.0 HB3 A:PRO407 3.7 13.7 1.0 CG2 A:ILE521 3.8 8.6 1.0 CZ A:TYR224 3.8 11.6 1.0 CZ A:ARG522 3.8 11.6 1.0 CE A:MET223 3.9 14.3 1.0 CG A:PRO407 3.9 13.2 1.0 CA A:ARG522 3.9 8.1 1.0 CG A:ARG522 4.0 10.8 1.0 HA A:ARG522 4.0 9.7 1.0 CD A:ARG522 4.2 10.7 1.0 HG2 A:PRO519 4.2 13.1 1.0 HG21 A:ILE521 4.2 10.3 1.0 HB2 A:ARG522 4.3 11.6 1.0 H A:ILE521 4.3 11.0 1.0 HH22 A:ARG522 4.3 15.1 1.0 C A:ILE521 4.5 9.6 1.0 CG A:PRO519 4.5 10.9 1.0 N A:ILE521 4.5 9.2 1.0 C A:PRO519 4.6 11.1 1.0 HG3 A:PRO407 4.6 15.8 1.0 HE2 A:MET223 4.6 17.2 1.0 HD2 A:PRO407 4.6 14.5 1.0 CA A:PRO519 4.7 10.2 1.0 O A:PRO519 4.7 11.3 1.0 HD2 A:ARG522 4.8 12.8 1.0 HD3 A:ARG522 4.8 12.8 1.0 N A:TYR520 4.8 9.4 1.0 O A:HOH1005 4.8 12.4 1.0 HB2 A:MET223 4.9 17.2 1.0 CA A:ILE521 4.9 9.9 1.0 CD A:PRO407 4.9 12.1 1.0 H A:TYR520 4.9 11.3 1.0 HG3 A:ARG522 4.9 12.9 1.0 CB A:ILE521 4.9 9.1 1.0 CD1 A:TYR224 4.9 11.9 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