Chlorine in PDB 7z6z: Crystal Structure of Angiotensin-1 Converting Enzyme N-Domain in Complex with Fosinoprilat

The structure of Crystal Structure of Angiotensin-1 Converting Enzyme N-Domain in Complex with Fosinoprilat, PDB code: 7z6z 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)	63.46 / 1.75
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	72.575, 77.8, 81.592, 88.92, 64.62, 74.81
R / Rfree (%)	17.2 / 20

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

Zinc	(Zn)	2 atoms
Sodium	(Na)	1 atom
Calcium	(Ca)	3 atoms

The binding sites of Chlorine atom in the Crystal Structure of Angiotensin-1 Converting Enzyme N-Domain in Complex with Fosinoprilat (pdb code 7z6z). 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 N-Domain in Complex with Fosinoprilat, PDB code: 7z6z:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of Angiotensin-1 Converting Enzyme N-Domain in Complex with Fosinoprilat


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 N-Domain in Complex with Fosinoprilat within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl719 b:19.9 occ:1.00 HE A:ARG500 2.3 23.6 1.0 HB3 A:ARG500 2.7 21.4 1.0 HH21 A:ARG500 2.8 26.7 1.0 HB2 A:PRO497 2.9 22.5 1.0 HB2 A:PRO385 3.0 23.1 1.0 OH A:TYR202 3.0 21.5 1.0 O A:HOH1026 3.1 20.2 1.0 H A:ARG500 3.1 20.4 1.0 HE1 A:TYR202 3.1 25.8 1.0 HG2 A:PRO385 3.1 25.7 1.0 NE A:ARG500 3.2 19.7 1.0 HE3 A:TRP201 3.2 29.2 1.0 HZ3 A:TRP201 3.3 31.3 1.0 HG22 A:ILE499 3.3 21.8 1.0 HG23 A:ILE499 3.5 21.8 1.0 NH2 A:ARG500 3.6 22.3 1.0 CB A:ARG500 3.6 17.9 1.0 HH A:TYR202 3.6 25.8 1.0 HB3 A:PRO497 3.7 22.5 1.0 CB A:PRO385 3.7 19.2 1.0 CB A:PRO497 3.7 18.8 1.0 N A:ARG500 3.8 17.0 1.0 CE1 A:TYR202 3.8 21.6 1.0 CZ A:ARG500 3.8 21.6 1.0 HG2 A:ARG500 3.8 22.2 1.0 HB3 A:PRO385 3.8 23.1 1.0 CG2 A:ILE499 3.8 18.2 1.0 CG A:PRO385 3.8 21.4 1.0 CZ A:TYR202 3.9 19.7 1.0 CE3 A:TRP201 3.9 24.4 1.0 CZ3 A:TRP201 3.9 26.1 1.0 CG A:ARG500 4.1 18.5 1.0 CA A:ARG500 4.1 16.8 1.0 HG2 A:PRO497 4.2 23.7 1.0 CD A:ARG500 4.2 19.8 1.0 HA A:ARG500 4.2 20.1 1.0 HB2 A:ARG500 4.3 21.4 1.0 HG21 A:ILE499 4.3 21.8 1.0 HH22 A:ARG500 4.3 26.7 1.0 H A:ILE499 4.4 22.4 1.0 HD2 A:PRO385 4.5 26.2 1.0 HG3 A:PRO385 4.5 25.7 1.0 CG A:PRO497 4.5 19.8 1.0 N A:ILE499 4.7 18.7 1.0 CD A:PRO385 4.8 21.9 1.0 C A:ILE499 4.8 17.8 1.0 HD3 A:ARG500 4.8 23.7 1.0 HD2 A:ARG500 4.8 23.7 1.0 C A:PRO497 4.8 18.8 1.0 O A:HOH951 4.9 21.3 1.0 CA A:PRO497 4.9 19.0 1.0 N A:TYR498 5.0 18.0 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of Angiotensin-1 Converting Enzyme N-Domain in Complex with Fosinoprilat


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 N-Domain in Complex with Fosinoprilat within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl714 b:24.9 occ:1.00 HE B:ARG500 2.3 31.2 1.0 HH B:TYR202 2.3 32.5 1.0 HB3 B:ARG500 2.7 31.2 1.0 HH21 B:ARG500 2.8 34.4 1.0 HB2 B:PRO497 2.9 29.4 1.0 HE2 B:TYR202 3.1 36.1 1.0 HB2 B:PRO385 3.1 34.5 1.0 H B:ARG500 3.1 27.9 1.0 HG22 B:ILE499 3.1 30.1 1.0 O B:HOH988 3.1 25.8 1.0 OH B:TYR202 3.2 27.1 1.0 NE B:ARG500 3.2 26.0 1.0 HE3 B:TRP201 3.2 42.5 1.0 HG2 B:PRO385 3.2 39.9 1.0 HZ3 B:TRP201 3.3 42.3 1.0 HG23 B:ILE499 3.6 30.1 1.0 NH2 B:ARG500 3.6 28.7 1.0 HB3 B:PRO497 3.6 29.4 1.0 CB B:ARG500 3.6 26.1 1.0 CB B:PRO497 3.6 24.6 1.0 CB B:PRO385 3.7 28.8 1.0 CE2 B:TYR202 3.7 30.1 1.0 CG2 B:ILE499 3.8 25.1 1.0 N B:ARG500 3.8 23.2 1.0 CZ B:ARG500 3.8 29.6 1.0 HB3 B:PRO385 3.8 34.5 1.0 CZ B:TYR202 3.9 28.0 1.0 HG2 B:ARG500 3.9 28.9 1.0 CE3 B:TRP201 3.9 35.5 1.0 CG B:PRO385 3.9 33.2 1.0 CZ3 B:TRP201 3.9 35.3 1.0 HG2 B:PRO497 4.1 29.7 1.0 CG B:ARG500 4.1 24.1 1.0 CA B:ARG500 4.2 25.3 1.0 CD B:ARG500 4.2 27.7 1.0 HG21 B:ILE499 4.2 30.1 1.0 HA B:ARG500 4.3 30.4 1.0 HB2 B:ARG500 4.3 31.2 1.0 HH22 B:ARG500 4.3 34.4 1.0 H B:ILE499 4.3 27.1 1.0 CG B:PRO497 4.4 24.8 1.0 HD2 B:PRO385 4.6 38.4 1.0 HG3 B:PRO385 4.6 39.9 1.0 N B:ILE499 4.7 22.6 1.0 HD2 B:ARG500 4.7 33.3 1.0 C B:PRO497 4.8 25.2 1.0 C B:ILE499 4.8 24.3 1.0 O B:HOH912 4.8 26.1 1.0 HD3 B:ARG500 4.8 33.3 1.0 CA B:PRO497 4.8 22.3 1.0 CD B:PRO385 4.8 32.0 1.0 N B:TYR498 5.0 21.4 1.0 H B:TYR498 5.0 25.6 1.0 HB3 B:TRP198 5.0 33.6 1.0

G.E.Cozier, E.C.Newby, S.L.U.Schwager, R.E.Isaac, E.D.Sturrock, K.R.Acharya. Structural Basis For the Inhibition of Human Angiotensin-1 Converting Enzyme By Fosinoprilat. Febs J. V. 289 6659 2022.
ISSN: ISSN 1742-464X
PubMed: 35653492
DOI: 10.1111/FEBS.16543