Chlorine in PDB 6h5w: Crystal Structure of Human Angiotensin-1 Converting Enzyme C-Domain in Complex with Omapatrilat.

All present enzymatic activity of Crystal Structure of Human Angiotensin-1 Converting Enzyme C-Domain in Complex with Omapatrilat.:
3.4.15.1;

The structure of Crystal Structure of Human Angiotensin-1 Converting Enzyme C-Domain in Complex with Omapatrilat., PDB code: 6h5w 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)	71.89 / 1.37
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	56.596, 85.126, 134.264, 90.00, 90.00, 90.00
R / Rfree (%)	14.5 / 17.5

The structure of Crystal Structure of Human Angiotensin-1 Converting Enzyme C-Domain in Complex with Omapatrilat. also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Chlorine atom in the Crystal Structure of Human Angiotensin-1 Converting Enzyme C-Domain in Complex with Omapatrilat. (pdb code 6h5w). 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 Human Angiotensin-1 Converting Enzyme C-Domain in Complex with Omapatrilat., PDB code: 6h5w:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of Human Angiotensin-1 Converting Enzyme C-Domain in Complex with Omapatrilat.


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 Human Angiotensin-1 Converting Enzyme C-Domain in Complex with Omapatrilat. within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl708 b:17.8 occ:1.00 HE A:ARG186 2.4 18.8 1.0 HH11 A:ARG186 2.5 20.2 1.0 HE1 A:TRP485 2.5 18.2 1.0 HH11 A:ARG489 2.8 18.4 1.0 HB3 A:ASP507 3.0 17.1 1.0 HZ2 A:TRP486 3.1 18.6 1.0 NE A:ARG186 3.2 15.7 1.0 O A:HOH1105 3.2 21.4 1.0 NH1 A:ARG489 3.3 15.3 1.0 NH1 A:ARG186 3.3 16.8 1.0 NE1 A:TRP485 3.4 15.2 1.0 HE A:ARG489 3.5 18.1 1.0 CZ2 A:TRP486 3.6 15.5 1.0 HH12 A:ARG489 3.6 18.4 1.0 CZ A:ARG186 3.7 15.2 1.0 HZ2 A:TRP485 3.8 19.5 1.0 CB A:ASP507 3.8 14.2 1.0 CZ A:ARG489 3.9 13.3 1.0 HZ2 A:TRP182 3.9 17.5 1.0 NE A:ARG489 3.9 15.1 1.0 HH2 A:TRP486 4.0 19.7 1.0 HB2 A:ASP507 4.0 17.1 1.0 HH12 A:ARG186 4.0 20.2 1.0 CH2 A:TRP486 4.1 16.4 1.0 CE2 A:TRP485 4.2 15.1 1.0 HD3 A:ARG186 4.3 17.5 1.0 CD A:ARG186 4.3 14.6 1.0 CD1 A:TRP485 4.3 15.5 1.0 HD1 A:TRP279 4.4 16.2 1.0 CE2 A:TRP486 4.4 14.2 1.0 CZ2 A:TRP485 4.4 16.3 1.0 HD1 A:TRP485 4.4 18.6 1.0 CZ2 A:TRP182 4.5 14.6 1.0 O A:ASP507 4.5 14.6 1.0 HE1 A:TRP486 4.6 16.8 1.0 HE1 A:TRP182 4.6 16.6 1.0 CG A:ASP507 4.7 14.8 1.0 HG2 A:ARG186 4.7 18.9 1.0 C A:ASP507 4.7 14.4 1.0 NE1 A:TRP486 4.8 14.0 1.0 CA A:ASP507 4.8 13.4 1.0 HA A:TRP279 4.8 15.6 1.0 O A:HOH1103 4.8 14.2 1.0 HG3 A:ARG489 4.9 18.3 1.0 HD3 A:ARG489 4.9 19.0 1.0 NH2 A:ARG489 4.9 13.0 1.0 HA A:ASP507 5.0 16.1 1.0 CD A:ARG489 5.0 15.8 1.0 OD2 A:ASP507 5.0 15.8 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of Human Angiotensin-1 Converting Enzyme C-Domain in Complex with Omapatrilat.


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 Human Angiotensin-1 Converting Enzyme C-Domain in Complex with Omapatrilat. within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl709 b:22.9 occ:1.00 HH A:TYR224 2.1 23.4 1.0 HE A:ARG522 2.4 21.3 1.0 HB3 A:ARG522 2.7 16.8 1.0 HH21 A:ARG522 2.8 24.5 1.0 H A:ARG522 2.8 16.4 1.0 HB2 A:PRO519 2.9 17.0 1.0 OH A:TYR224 2.9 19.5 1.0 HE1 A:TYR224 3.0 17.7 1.0 HG22 A:ILE521 3.0 20.3 1.0 O A:HOH1180 3.0 24.7 1.0 HB2 A:PRO407 3.2 20.2 1.0 NE A:ARG522 3.3 17.7 1.0 HG2 A:PRO407 3.4 20.6 1.0 N A:ARG522 3.5 13.7 1.0 NH2 A:ARG522 3.5 20.4 1.0 HB3 A:PRO519 3.5 17.0 1.0 CB A:ARG522 3.5 14.0 1.0 HG23 A:ILE521 3.6 20.3 1.0 CE1 A:TYR224 3.6 14.8 1.0 CB A:PRO519 3.6 14.2 1.0 CZ A:TYR224 3.7 15.1 1.0 CG2 A:ILE521 3.7 16.9 1.0 HG2 A:ARG522 3.7 17.7 1.0 CB A:PRO407 3.9 16.9 1.0 CZ A:ARG522 3.9 20.6 1.0 CA A:ARG522 3.9 13.0 1.0 HA A:ARG522 3.9 15.6 1.0 HB3 A:PRO407 4.0 20.2 1.0 CG A:ARG522 4.0 14.8 1.0 CG A:PRO407 4.1 17.2 1.0 H A:ILE521 4.1 14.8 1.0 HG21 A:ILE521 4.2 20.3 1.0 HG2 A:PRO519 4.3 16.9 1.0 HH22 A:ARG522 4.3 24.5 1.0 CD A:ARG522 4.3 15.9 1.0 HB2 A:ARG522 4.3 16.8 1.0 C A:ILE521 4.4 13.2 1.0 N A:ILE521 4.5 12.4 1.0 CG A:PRO519 4.6 14.1 1.0 O A:HOH1021 4.6 18.5 1.0 HD2 A:PRO407 4.6 18.7 1.0 C A:PRO519 4.7 12.2 1.0 HG3 A:PRO407 4.8 20.6 1.0 CA A:PRO519 4.8 12.8 1.0 CA A:ILE521 4.8 12.8 1.0 SD A:MET223 4.8 27.4 1.0 CD1 A:TYR224 4.8 15.3 1.0 HD2 A:ARG522 4.8 19.0 1.0 CB A:ILE521 4.9 16.1 1.0 N A:TYR520 4.9 12.8 1.0 HB2 A:MET223 4.9 23.4 1.0 O A:PRO519 4.9 13.9 1.0 HD3 A:ARG522 4.9 19.0 1.0 H A:TYR520 4.9 15.3 1.0 CE2 A:TYR224 5.0 16.3 1.0 CD A:PRO407 5.0 15.6 1.0 HG3 A:ARG522 5.0 17.7 1.0

G.E.Cozier, L.B.Arendse, S.L.Schwager, E.D.Sturrock, K.R.Acharya. Molecular Basis For Multiple Omapatrilat Binding Sites Within the Ace C-Domain: Implications For Drug Design. J. Med. Chem. V. 61 10141 2018.
ISSN: ISSN 1520-4804
PubMed: 30372620
DOI: 10.1021/ACS.JMEDCHEM.8B01309