Chlorine in PDB 7z70: Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain in Complex with Fosinoprilat

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

The structure of Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain in Complex with Fosinoprilat, PDB code: 7z70 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)	52.15 / 1.85
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	56.563, 85.987, 134.686, 90, 90, 90
R / Rfree (%)	17.4 / 21.3

The structure of Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain in Complex with Fosinoprilat 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 Fosinoprilat (pdb code 7z70). 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 Fosinoprilat, PDB code: 7z70:
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 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 C-Domain in Complex with Fosinoprilat within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl711 b:17.9 occ:1.00 HE A:ARG186 2.4 20.4 1.0 HE1 A:TRP485 2.4 21.6 1.0 HH21 A:ARG186 2.5 20.8 1.0 HH21 A:ARG489 2.7 21.6 1.0 HB3 A:ASP507 2.9 19.4 1.0 HZ2 A:TRP486 3.1 19.1 1.0 NE A:ARG186 3.2 17.0 1.0 NH2 A:ARG489 3.2 18.0 1.0 NH2 A:ARG186 3.3 17.3 1.0 NE1 A:TRP485 3.3 18.0 1.0 HE A:ARG489 3.4 19.7 1.0 O A:HOH967 3.4 20.4 1.0 CZ2 A:TRP486 3.6 15.9 1.0 HH22 A:ARG489 3.6 21.6 1.0 CZ A:ARG186 3.7 15.3 1.0 NE A:ARG489 3.8 16.4 1.0 CB A:ASP507 3.8 16.1 1.0 HZ2 A:TRP485 3.8 20.5 1.0 CZ A:ARG489 3.8 14.0 1.0 HZ2 A:TRP182 3.8 16.6 1.0 HB2 A:ASP507 3.9 19.4 1.0 HH22 A:ARG186 4.0 20.8 1.0 HH2 A:TRP486 4.0 19.6 1.0 CH2 A:TRP486 4.1 16.3 1.0 CE2 A:TRP485 4.2 16.7 1.0 HD3 A:ARG186 4.3 20.5 1.0 CD1 A:TRP485 4.3 15.3 1.0 CE2 A:TRP486 4.3 14.2 1.0 CZ2 A:TRP485 4.3 17.1 1.0 CD A:ARG186 4.3 17.1 1.0 HD1 A:TRP485 4.4 18.4 1.0 HD1 A:TRP279 4.4 17.1 1.0 O A:ASP507 4.5 17.5 1.0 CZ2 A:TRP182 4.5 13.9 1.0 HE1 A:TRP486 4.5 17.1 1.0 CG A:ASP507 4.6 16.7 1.0 HE1 A:TRP182 4.6 21.0 1.0 C A:ASP507 4.7 16.0 1.0 HG3 A:ARG489 4.7 17.6 1.0 NE1 A:TRP486 4.7 14.2 1.0 HG2 A:ARG186 4.7 20.3 1.0 HD3 A:ARG489 4.8 18.1 1.0 CA A:ASP507 4.8 16.2 1.0 CD A:ARG489 4.8 15.1 1.0 HA A:TRP279 4.9 17.8 1.0 NH1 A:ARG489 4.9 15.8 1.0 O A:HOH981 4.9 17.1 1.0 OD2 A:ASP507 4.9 17.7 1.0 HA A:ASP507 5.0 19.4 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of Angiotensin-1 Converting Enzyme C-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 C-Domain in Complex with Fosinoprilat within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl712 b:19.1 occ:1.00 HE A:ARG522 2.4 16.3 1.0 HB3 A:ARG522 2.7 14.8 1.0 HB2 A:PRO519 2.9 15.8 1.0 HH21 A:ARG522 2.9 21.2 1.0 H A:ARG522 2.9 16.1 1.0 HE1 A:TYR224 3.0 19.9 1.0 O A:HOH1037 3.0 17.6 1.0 OH A:TYR224 3.0 15.4 1.0 HB2 A:PRO407 3.0 20.3 1.0 HG22 A:ILE521 3.0 22.7 1.0 HG2 A:PRO407 3.2 19.9 1.0 NE A:ARG522 3.2 13.6 1.0 HG23 A:ILE521 3.4 22.7 1.0 CB A:ARG522 3.5 12.3 1.0 N A:ARG522 3.6 13.4 1.0 CE1 A:TYR224 3.6 16.6 1.0 HH A:TYR224 3.6 18.5 1.0 HB3 A:PRO519 3.6 15.8 1.0 CB A:PRO407 3.7 16.9 1.0 NH2 A:ARG522 3.7 17.6 1.0 CB A:PRO519 3.7 13.2 1.0 CG2 A:ILE521 3.7 18.9 1.0 HG2 A:ARG522 3.7 16.3 1.0 CZ A:TYR224 3.7 16.1 1.0 HB3 A:PRO407 3.8 20.3 1.0 CG A:PRO407 3.8 16.6 1.0 CZ A:ARG522 3.9 17.6 1.0 CA A:ARG522 4.0 13.0 1.0 CG A:ARG522 4.0 13.6 1.0 HA A:ARG522 4.0 15.6 1.0 HG2 A:PRO519 4.1 17.0 1.0 HG21 A:ILE521 4.1 22.7 1.0 H A:ILE521 4.2 14.4 1.0 CD A:ARG522 4.2 13.4 1.0 HB2 A:ARG522 4.3 14.8 1.0 SD A:MET223 4.4 26.6 1.0 HH22 A:ARG522 4.4 21.2 1.0 CG A:PRO519 4.5 14.2 1.0 HD2 A:PRO407 4.5 21.4 1.0 HG3 A:PRO407 4.5 19.9 1.0 N A:ILE521 4.5 12.0 1.0 HE1 A:MET223 4.5 32.7 1.0 C A:ILE521 4.6 12.6 1.0 HB2 A:MET223 4.7 22.5 1.0 C A:PRO519 4.7 16.4 1.0 HE2 A:MET223 4.8 32.7 1.0 HD3 A:ARG522 4.8 16.1 1.0 CD A:PRO407 4.8 17.8 1.0 HD2 A:ARG522 4.8 16.1 1.0 CD1 A:TYR224 4.8 16.4 1.0 CE A:MET223 4.8 27.3 1.0 CA A:PRO519 4.8 13.1 1.0 O A:HOH1003 4.8 14.7 1.0 CB A:ILE521 4.9 14.1 1.0 CA A:ILE521 4.9 14.1 1.0 O A:PRO519 4.9 11.6 1.0 HG3 A:ARG522 4.9 16.3 1.0 N A:TYR520 5.0 14.3 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