Chlorine in PDB 6h5x: Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Omapatrilat.

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

The structure of Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Omapatrilat., PDB code: 6h5x 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)	44.60 / 1.80
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	73.160, 76.953, 83.088, 88.83, 64.22, 75.21
R / Rfree (%)	16.4 / 20.4

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

Magnesium	(Mg)	1 atom
Zinc	(Zn)	2 atoms

The binding sites of Chlorine atom in the Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Omapatrilat. (pdb code 6h5x). 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 N-Domain in Complex with Omapatrilat., PDB code: 6h5x:
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 N-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 N-Domain in Complex with Omapatrilat. within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl710 b:28.6 occ:1.00 HH A:TYR202 2.2 37.3 1.0 HE A:ARG500 2.4 32.6 1.0 HB3 A:ARG500 2.8 28.3 1.0 HH21 A:ARG500 2.9 35.1 1.0 HB2 A:PRO497 3.0 31.1 1.0 O A:HOH1015 3.0 31.3 1.0 OH A:TYR202 3.0 31.1 1.0 HB2 A:PRO385 3.1 37.7 1.0 HE1 A:TYR202 3.1 38.5 1.0 H A:ARG500 3.1 26.7 1.0 HG22 A:ILE499 3.2 30.3 1.0 HE3 A:TRP201 3.2 43.1 1.0 NE A:ARG500 3.2 27.1 1.0 HG2 A:PRO385 3.2 37.8 1.0 HZ3 A:TRP201 3.3 42.1 1.0 HG23 A:ILE499 3.6 30.3 1.0 NH2 A:ARG500 3.6 29.3 1.0 CB A:ARG500 3.6 23.6 1.0 HB3 A:PRO497 3.7 31.1 1.0 N A:ARG500 3.7 22.2 1.0 CB A:PRO385 3.7 31.4 1.0 CE1 A:TYR202 3.7 32.1 1.0 CB A:PRO497 3.7 25.9 1.0 HG2 A:ARG500 3.8 30.1 1.0 CZ A:TYR202 3.8 31.8 1.0 CG2 A:ILE499 3.8 25.2 1.0 HB3 A:PRO385 3.9 37.7 1.0 CE3 A:TRP201 3.9 35.9 1.0 CZ A:ARG500 3.9 29.2 1.0 CZ3 A:TRP201 3.9 35.1 1.0 CG A:PRO385 3.9 31.5 1.0 CG A:ARG500 4.1 25.1 1.0 CA A:ARG500 4.1 22.8 1.0 HA A:ARG500 4.1 27.3 1.0 HG2 A:PRO497 4.2 33.5 1.0 CD A:ARG500 4.2 26.7 1.0 HG21 A:ILE499 4.3 30.3 1.0 HB2 A:ARG500 4.4 28.3 1.0 HH22 A:ARG500 4.4 35.1 1.0 H A:ILE499 4.4 29.8 1.0 HD2 A:PRO385 4.5 38.4 1.0 CG A:PRO497 4.6 27.9 1.0 HG3 A:PRO385 4.6 37.8 1.0 C A:ILE499 4.7 22.9 1.0 N A:ILE499 4.7 24.9 1.0 O A:HOH953 4.7 29.2 1.0 HD2 A:ARG500 4.8 32.1 1.0 CD A:PRO385 4.8 32.0 1.0 C A:PRO497 4.8 24.7 1.0 HD3 A:ARG500 4.8 32.1 1.0 HB3 A:TRP198 4.9 40.5 1.0 CA A:PRO497 4.9 25.5 1.0 N A:TYR498 5.0 23.8 1.0 H A:TYR498 5.0 28.5 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of Human Angiotensin-1 Converting Enzyme N-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 N-Domain in Complex with Omapatrilat. within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl712 b:25.6 occ:1.00 HH B:TYR202 2.3 28.0 1.0 HE B:ARG500 2.3 28.0 1.0 HB3 B:ARG500 2.7 23.0 1.0 HH21 B:ARG500 2.8 29.0 1.0 HB2 B:PRO497 3.0 26.1 1.0 HB2 B:PRO385 3.1 28.7 1.0 HE2 B:TYR202 3.1 30.6 1.0 O B:HOH1071 3.1 23.8 1.0 OH B:TYR202 3.1 23.4 1.0 HG22 B:ILE499 3.1 24.3 1.0 H B:ARG500 3.1 22.9 1.0 NE B:ARG500 3.2 23.4 1.0 HE3 B:TRP201 3.3 34.1 1.0 HG2 B:PRO385 3.3 28.9 1.0 HZ3 B:TRP201 3.3 33.0 1.0 NH2 B:ARG500 3.5 24.1 1.0 CB B:ARG500 3.6 19.2 1.0 HG2 B:ARG500 3.7 25.7 1.0 HG23 B:ILE499 3.7 24.3 1.0 N B:ARG500 3.7 19.1 1.0 HB3 B:PRO497 3.7 26.1 1.0 CE2 B:TYR202 3.7 25.5 1.0 CB B:PRO385 3.7 23.9 1.0 CB B:PRO497 3.8 21.7 1.0 CZ B:ARG500 3.8 25.1 1.0 CG2 B:ILE499 3.8 20.2 1.0 CZ B:TYR202 3.9 24.1 1.0 HB3 B:PRO385 3.9 28.7 1.0 CE3 B:TRP201 3.9 28.4 1.0 CG B:PRO385 4.0 24.1 1.0 CZ3 B:TRP201 4.0 27.5 1.0 CG B:ARG500 4.0 21.4 1.0 CA B:ARG500 4.1 18.7 1.0 HA B:ARG500 4.1 22.5 1.0 CD B:ARG500 4.2 23.0 1.0 HG21 B:ILE499 4.2 24.3 1.0 HG2 B:PRO497 4.3 27.5 1.0 HH22 B:ARG500 4.3 29.0 1.0 HB2 B:ARG500 4.3 23.0 1.0 H B:ILE499 4.4 24.6 1.0 HD2 B:PRO385 4.4 28.4 1.0 CG B:PRO497 4.6 22.9 1.0 C B:ILE499 4.7 20.4 1.0 HG3 B:PRO385 4.7 28.9 1.0 N B:ILE499 4.7 20.5 1.0 HD2 B:ARG500 4.8 27.6 1.0 C B:PRO497 4.8 21.6 1.0 CD B:PRO385 4.8 23.6 1.0 HD3 B:ARG500 4.8 27.6 1.0 O B:HOH1034 4.8 21.5 1.0 CA B:PRO497 4.9 21.4 1.0 HG3 B:ARG500 5.0 25.7 1.0 O B:PRO497 5.0 21.4 1.0 N B:TYR498 5.0 20.4 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