Chlorine in PDB 6f9u: Crystal Structure of Human Testis Angiotensin-1 Converting Enzyme in Complex with Sampatrilat-Asp.

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

The structure of Crystal Structure of Human Testis Angiotensin-1 Converting Enzyme in Complex with Sampatrilat-Asp., PDB code: 6f9u 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)	72.17 / 1.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	56.316, 85.861, 133.233, 90.00, 90.00, 90.00
R / Rfree (%)	16.7 / 20.9

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

Zinc

(Zn)

1 atom

The binding sites of Chlorine atom in the Crystal Structure of Human Testis Angiotensin-1 Converting Enzyme in Complex with Sampatrilat-Asp. (pdb code 6f9u). 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 Testis Angiotensin-1 Converting Enzyme in Complex with Sampatrilat-Asp., PDB code: 6f9u:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of Human Testis Angiotensin-1 Converting Enzyme 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 Testis Angiotensin-1 Converting Enzyme in Complex with Sampatrilat-Asp. within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl708 b:21.8 occ:1.00 HE A:ARG186 2.4 23.6 1.0 HE1 A:TRP485 2.5 24.4 1.0 HH11 A:ARG186 2.6 27.4 1.0 HH11 A:ARG489 2.7 25.9 1.0 HB3 A:ASP507 2.9 22.1 1.0 HZ2 A:TRP486 3.0 21.5 1.0 NH1 A:ARG489 3.2 21.6 1.0 NE A:ARG186 3.3 19.6 1.0 O A:HOH1028 3.3 26.4 1.0 NE1 A:TRP485 3.3 20.4 1.0 HE A:ARG489 3.4 23.1 1.0 NH1 A:ARG186 3.4 22.9 1.0 CZ2 A:TRP486 3.5 17.9 1.0 HZ2 A:TRP182 3.7 17.8 1.0 HH12 A:ARG489 3.7 25.9 1.0 CZ A:ARG186 3.8 18.6 1.0 NE A:ARG489 3.8 19.3 1.0 HZ2 A:TRP485 3.8 27.1 1.0 CB A:ASP507 3.8 18.4 1.0 HH2 A:TRP486 3.8 23.1 1.0 CZ A:ARG489 3.8 19.8 1.0 CH2 A:TRP486 3.9 19.3 1.0 HB2 A:ASP507 4.0 22.1 1.0 HH12 A:ARG186 4.1 27.4 1.0 CE2 A:TRP485 4.2 19.1 1.0 HD3 A:ARG186 4.3 22.5 1.0 CD1 A:TRP485 4.3 16.9 1.0 CE2 A:TRP486 4.3 14.1 1.0 CZ2 A:TRP182 4.3 14.9 1.0 CZ2 A:TRP485 4.4 22.6 1.0 HD1 A:TRP485 4.4 20.3 1.0 CD A:ARG186 4.4 18.8 1.0 HD1 A:TRP279 4.5 24.6 1.0 HE1 A:TRP182 4.5 22.2 1.0 HE1 A:TRP486 4.6 19.8 1.0 O A:ASP507 4.6 18.4 1.0 CG A:ASP507 4.6 18.7 1.0 O A:HOH937 4.7 19.2 1.0 HG2 A:ARG186 4.8 21.1 1.0 NE1 A:TRP486 4.8 16.5 1.0 C A:ASP507 4.8 19.3 1.0 CA A:ASP507 4.8 20.0 1.0 HG3 A:ARG489 4.8 24.3 1.0 HA A:TRP279 4.9 21.2 1.0 NH2 A:ARG489 4.9 18.4 1.0 HD3 A:ARG489 4.9 22.7 1.0 CE2 A:TRP182 4.9 23.0 1.0 CD A:ARG489 4.9 18.9 1.0 NE1 A:TRP182 5.0 18.5 1.0 OD2 A:ASP507 5.0 18.3 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of Human Testis Angiotensin-1 Converting Enzyme 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 Testis Angiotensin-1 Converting Enzyme in Complex with Sampatrilat-Asp. within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl709 b:22.7 occ:1.00 HH A:TYR224 2.3 27.9 1.0 HE A:ARG522 2.4 26.8 1.0 HB3 A:ARG522 2.7 21.1 1.0 H A:ARG522 2.8 21.1 1.0 HB2 A:PRO519 2.8 22.9 1.0 HH21 A:ARG522 2.9 26.3 1.0 OH A:TYR224 3.0 23.3 1.0 HE1 A:TYR224 3.1 26.2 1.0 O A:HOH999 3.1 23.9 1.0 HG22 A:ILE521 3.1 23.5 1.0 HB2 A:PRO407 3.1 22.6 1.0 HE3 A:MET223 3.2 33.2 1.0 NE A:ARG522 3.3 22.3 1.0 HG2 A:PRO407 3.3 25.9 1.0 N A:ARG522 3.5 17.6 1.0 HE1 A:MET223 3.5 33.2 1.0 CB A:ARG522 3.6 17.6 1.0 NH2 A:ARG522 3.6 21.9 1.0 CB A:PRO519 3.6 19.1 1.0 HB3 A:PRO519 3.6 22.9 1.0 HG23 A:ILE521 3.7 23.5 1.0 CE1 A:TYR224 3.7 21.9 1.0 CB A:PRO407 3.7 18.8 1.0 HB3 A:PRO407 3.8 22.6 1.0 CG2 A:ILE521 3.8 19.6 1.0 CE A:MET223 3.8 27.7 1.0 CZ A:TYR224 3.8 20.8 1.0 HG2 A:ARG522 3.8 22.0 1.0 CZ A:ARG522 3.9 22.8 1.0 CA A:ARG522 3.9 16.2 1.0 HA A:ARG522 4.0 19.4 1.0 CG A:PRO407 4.0 21.6 1.0 CG A:ARG522 4.1 18.3 1.0 H A:ILE521 4.2 15.9 1.0 HG2 A:PRO519 4.2 26.6 1.0 HE2 A:MET223 4.2 33.2 1.0 CD A:ARG522 4.3 21.2 1.0 HB2 A:ARG522 4.3 21.1 1.0 HG21 A:ILE521 4.4 23.5 1.0 HH22 A:ARG522 4.4 26.3 1.0 C A:ILE521 4.4 16.2 1.0 N A:ILE521 4.5 13.3 1.0 C A:PRO519 4.5 18.6 1.0 CG A:PRO519 4.5 22.1 1.0 HG3 A:PRO407 4.6 25.9 1.0 O A:PRO519 4.6 19.8 1.0 CA A:PRO519 4.7 15.3 1.0 O A:HOH930 4.7 18.8 1.0 HD2 A:PRO407 4.8 25.9 1.0 N A:TYR520 4.8 17.7 1.0 CA A:ILE521 4.8 13.3 1.0 HD2 A:ARG522 4.8 25.5 1.0 CB A:ILE521 4.9 16.3 1.0 HD3 A:ARG522 4.9 25.5 1.0 H A:TYR520 4.9 21.2 1.0 CD1 A:TYR224 4.9 18.8 1.0 HB2 A:MET223 5.0 24.0 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