Chlorine in PDB 6f9r: Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Sampatrilat-Asp.

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

The structure of Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Sampatrilat-Asp., PDB code: 6f9r 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)	44.39 / 1.85
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	72.591, 76.966, 82.637, 88.43, 64.40, 75.32
R / Rfree (%)	19.8 / 22.8

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

Magnesium	(Mg)	3 atoms
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 Sampatrilat-Asp. (pdb code 6f9r). 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 Sampatrilat-Asp., PDB code: 6f9r:
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 Sampatrilat-Asp.


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 Sampatrilat-Asp. within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl711 b:26.7 occ:1.00 HH A:TYR202 2.3 35.2 1.0 HE A:ARG500 2.3 29.8 1.0 HH21 A:ARG500 2.7 39.4 1.0 HB3 A:ARG500 2.8 23.1 1.0 HB2 A:PRO497 2.8 30.6 1.0 H A:ARG500 3.1 25.5 1.0 O A:HOH1028 3.1 29.8 1.0 OH A:TYR202 3.1 29.3 1.0 NE A:ARG500 3.1 24.8 1.0 HG22 A:ILE499 3.2 25.0 1.0 HB2 A:PRO385 3.2 35.0 1.0 HE1 A:TYR202 3.2 38.1 1.0 HE3 A:TRP201 3.2 44.6 1.0 HZ3 A:TRP201 3.3 41.7 1.0 HG2 A:PRO385 3.3 42.4 1.0 NH2 A:ARG500 3.5 32.8 1.0 CB A:ARG500 3.6 19.2 1.0 HG23 A:ILE499 3.6 25.0 1.0 CB A:PRO497 3.7 25.4 1.0 HG2 A:ARG500 3.7 31.5 1.0 N A:ARG500 3.7 21.2 1.0 CZ A:ARG500 3.8 31.5 1.0 HB3 A:PRO497 3.8 30.6 1.0 CB A:PRO385 3.8 29.2 1.0 CG2 A:ILE499 3.8 20.8 1.0 CE1 A:TYR202 3.9 31.7 1.0 HB3 A:PRO385 3.9 35.0 1.0 CE3 A:TRP201 3.9 37.2 1.0 HG2 A:PRO497 3.9 34.6 1.0 CZ A:TYR202 3.9 34.0 1.0 CZ3 A:TRP201 3.9 34.7 1.0 CG A:PRO385 4.0 35.3 1.0 CG A:ARG500 4.0 26.3 1.0 CA A:ARG500 4.1 21.0 1.0 CD A:ARG500 4.2 30.1 1.0 HA A:ARG500 4.2 25.2 1.0 HH22 A:ARG500 4.2 39.4 1.0 HG21 A:ILE499 4.3 25.0 1.0 H A:ILE499 4.3 22.2 1.0 HB2 A:ARG500 4.4 23.1 1.0 CG A:PRO497 4.4 28.8 1.0 HG3 A:PRO385 4.6 42.4 1.0 C A:PRO497 4.7 25.8 1.0 N A:ILE499 4.7 18.5 1.0 HD2 A:PRO385 4.7 45.0 1.0 HD2 A:ARG500 4.7 36.1 1.0 C A:ILE499 4.7 21.2 1.0 HD3 A:ARG500 4.8 36.1 1.0 CA A:PRO497 4.8 24.4 1.0 O A:PRO497 4.8 20.6 1.0 N A:TYR498 4.9 19.7 1.0 O A:HOH876 4.9 25.0 1.0 HD2 A:PRO497 4.9 37.0 1.0 H A:TYR498 4.9 23.7 1.0 HG3 A:ARG500 5.0 31.5 1.0 CD A:PRO385 5.0 37.5 1.0 HB3 A:TRP198 5.0 35.2 1.0

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


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 Sampatrilat-Asp. within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl712 b:24.1 occ:1.00 HH B:TYR202 2.2 27.2 1.0 HE B:ARG500 2.4 36.8 1.0 HB3 B:ARG500 2.7 25.2 1.0 HB2 B:PRO497 2.9 30.3 1.0 HH21 B:ARG500 2.9 39.0 1.0 H B:ARG500 3.0 24.8 1.0 OH B:TYR202 3.0 22.6 1.0 HG2 B:PRO385 3.0 37.4 1.0 HB2 B:PRO385 3.1 49.3 1.0 O B:HOH1034 3.1 23.1 1.0 HE2 B:TYR202 3.2 30.5 1.0 HG22 B:ILE499 3.2 26.0 1.0 HE3 B:TRP201 3.3 40.7 1.0 NE B:ARG500 3.3 30.6 1.0 HZ3 B:TRP201 3.3 44.8 1.0 CB B:ARG500 3.6 21.0 1.0 NH2 B:ARG500 3.6 32.5 1.0 HG23 B:ILE499 3.6 26.0 1.0 N B:ARG500 3.6 20.6 1.0 CB B:PRO497 3.7 25.3 1.0 CB B:PRO385 3.7 41.1 1.0 HB3 B:PRO497 3.7 30.3 1.0 CG B:PRO385 3.7 31.1 1.0 CE2 B:TYR202 3.8 25.4 1.0 CZ B:TYR202 3.8 25.5 1.0 HG2 B:ARG500 3.8 29.2 1.0 HB3 B:PRO385 3.8 49.3 1.0 CG2 B:ILE499 3.8 21.6 1.0 CZ B:ARG500 3.9 40.0 1.0 CE3 B:TRP201 3.9 33.9 1.0 CZ3 B:TRP201 4.0 37.3 1.0 CA B:ARG500 4.0 21.8 1.0 CG B:ARG500 4.1 24.3 1.0 HA B:ARG500 4.1 26.2 1.0 HG2 B:PRO497 4.1 32.5 1.0 H B:ILE499 4.2 25.4 1.0 HB2 B:ARG500 4.3 25.2 1.0 CD B:ARG500 4.3 31.2 1.0 HH22 B:ARG500 4.3 39.0 1.0 HG21 B:ILE499 4.3 26.0 1.0 HG3 B:PRO385 4.3 37.4 1.0 HD2 B:PRO385 4.5 37.0 1.0 CG B:PRO497 4.5 27.0 1.0 N B:ILE499 4.6 21.2 1.0 C B:ILE499 4.7 19.2 1.0 C B:PRO497 4.7 25.9 1.0 CD B:PRO385 4.7 30.8 1.0 CA B:PRO497 4.8 22.1 1.0 HD2 B:ARG500 4.8 37.4 1.0 N B:TYR498 4.8 21.1 1.0 O B:HOH917 4.9 23.0 1.0 H B:TYR498 4.9 25.3 1.0 HD3 B:ARG500 4.9 37.4 1.0 O B:PRO497 4.9 18.7 1.0 CA B:ILE499 5.0 16.4 1.0

G.E.Cozier, S.L.Schwager, R.K.Sharma, K.Chibale, E.D.Sturrock, K.R.Acharya. Crystal Structures of Sampatrilat and Sampatrilat-Asp in Complex with Human Ace - A Molecular Basis For Domain Selectivity. Febs J. V. 285 1477 2018.
ISSN: ISSN 1742-4658
PubMed: 29476645
DOI: 10.1111/FEBS.14421