Chlorine in PDB 6f9t: Crystal Structure of Human Testis Angiotensin-1 Converting Enzyme in Complex with Sampatrilat.

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

The structure of Crystal Structure of Human Testis Angiotensin-1 Converting Enzyme in Complex with Sampatrilat., PDB code: 6f9t 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)	71.63 / 1.60
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	57.105, 84.763, 133.957, 90.00, 90.00, 90.00
R / Rfree (%)	16.5 / 18.7

The structure of Crystal Structure of Human Testis Angiotensin-1 Converting Enzyme in Complex with Sampatrilat. 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. (pdb code 6f9t). 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., PDB code: 6f9t:
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.


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. within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl713 b:14.3 occ:1.00 HE A:ARG186 2.4 14.0 1.0 HE1 A:TRP485 2.5 13.2 1.0 HH11 A:ARG186 2.5 14.5 1.0 HH11 A:ARG489 2.8 13.4 1.0 HB3 A:ASP507 3.0 11.8 1.0 HZ2 A:TRP486 3.0 13.5 1.0 O A:HOH1174 3.2 14.7 1.0 NE A:ARG186 3.2 11.6 1.0 NH1 A:ARG489 3.2 11.2 1.0 NH1 A:ARG186 3.3 12.1 1.0 NE1 A:TRP485 3.3 11.0 1.0 HE A:ARG489 3.5 13.1 1.0 CZ2 A:TRP486 3.5 11.2 1.0 HH12 A:ARG489 3.7 13.4 1.0 CZ A:ARG186 3.7 11.7 1.0 CZ A:ARG489 3.8 9.9 1.0 NE A:ARG489 3.8 10.9 1.0 HZ2 A:TRP182 3.8 13.1 1.0 CB A:ASP507 3.9 9.8 1.0 HZ2 A:TRP485 3.9 15.6 1.0 HH2 A:TRP486 3.9 13.5 1.0 CH2 A:TRP486 4.0 11.3 1.0 HB2 A:ASP507 4.0 11.8 1.0 HH12 A:ARG186 4.0 14.5 1.0 CE2 A:TRP485 4.2 10.5 1.0 HD3 A:ARG186 4.3 12.2 1.0 CD1 A:TRP485 4.3 10.8 1.0 CE2 A:TRP486 4.3 9.8 1.0 CD A:ARG186 4.4 10.1 1.0 HD1 A:TRP485 4.4 13.0 1.0 CZ2 A:TRP485 4.4 13.0 1.0 CZ2 A:TRP182 4.5 10.9 1.0 HD1 A:TRP279 4.5 11.7 1.0 HE1 A:TRP486 4.5 12.0 1.0 HE1 A:TRP182 4.5 12.7 1.0 O A:ASP507 4.6 11.2 1.0 CG A:ASP507 4.6 10.0 1.0 NE1 A:TRP486 4.7 10.0 1.0 HG2 A:ARG186 4.7 13.4 1.0 HG3 A:ARG489 4.8 12.9 1.0 C A:ASP507 4.8 11.1 1.0 HD3 A:ARG489 4.8 13.9 1.0 O A:HOH1122 4.8 9.7 1.0 NH2 A:ARG489 4.8 9.8 1.0 CA A:ASP507 4.9 10.4 1.0 CD A:ARG489 4.9 11.6 1.0 HA A:TRP279 4.9 11.5 1.0 OD2 A:ASP507 5.0 11.8 1.0 NE1 A:TRP182 5.0 10.5 1.0

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


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. within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl714 b:12.4 occ:1.00 HH A:TYR224 2.2 12.2 1.0 HE A:ARG522 2.3 13.7 1.0 HB3 A:ARG522 2.7 11.4 1.0 HH21 A:ARG522 2.8 18.8 1.0 HB2 A:PRO519 2.9 13.7 1.0 H A:ARG522 2.9 10.7 1.0 OH A:TYR224 3.0 10.1 1.0 HE1 A:TYR224 3.0 12.9 1.0 O A:HOH1163 3.1 13.6 1.0 HG22 A:ILE521 3.1 12.6 1.0 HB2 A:PRO407 3.2 14.5 1.0 NE A:ARG522 3.2 11.4 1.0 HG2 A:PRO407 3.4 13.3 1.0 HE3 A:MET223 3.5 15.3 1.0 NH2 A:ARG522 3.5 15.7 1.0 N A:ARG522 3.5 8.9 1.0 CB A:ARG522 3.6 9.5 1.0 HG23 A:ILE521 3.6 12.6 1.0 HB3 A:PRO519 3.6 13.7 1.0 CB A:PRO519 3.7 11.4 1.0 CE1 A:TYR224 3.7 10.8 1.0 HE1 A:MET223 3.7 15.3 1.0 HG2 A:ARG522 3.7 12.0 1.0 CG2 A:ILE521 3.8 10.4 1.0 CZ A:TYR224 3.8 10.4 1.0 CZ A:ARG522 3.8 14.3 1.0 CB A:PRO407 3.8 12.1 1.0 HB3 A:PRO407 3.9 14.5 1.0 CA A:ARG522 4.0 8.4 1.0 HA A:ARG522 4.0 10.1 1.0 CG A:ARG522 4.0 10.0 1.0 CE A:MET223 4.0 12.7 1.0 CG A:PRO407 4.1 11.1 1.0 H A:ILE521 4.2 11.4 1.0 CD A:ARG522 4.2 11.0 1.0 HG21 A:ILE521 4.2 12.6 1.0 HH22 A:ARG522 4.3 18.8 1.0 HB2 A:ARG522 4.3 11.4 1.0 HG2 A:PRO519 4.3 15.0 1.0 N A:ILE521 4.5 9.4 1.0 C A:ILE521 4.5 9.0 1.0 C A:PRO519 4.6 10.1 1.0 HE2 A:MET223 4.6 15.3 1.0 HD2 A:PRO407 4.6 13.9 1.0 CG A:PRO519 4.6 12.5 1.0 HG3 A:PRO407 4.7 13.3 1.0 O A:PRO519 4.8 9.7 1.0 CA A:PRO519 4.8 10.7 1.0 N A:TYR520 4.8 9.3 1.0 HD3 A:ARG522 4.8 13.2 1.0 O A:HOH1060 4.8 10.9 1.0 HD2 A:ARG522 4.8 13.2 1.0 CA A:ILE521 4.9 9.4 1.0 H A:TYR520 4.9 11.2 1.0 HB2 A:MET223 4.9 14.7 1.0 CB A:ILE521 4.9 8.8 1.0 CD1 A:TYR224 4.9 10.5 1.0 CD A:PRO407 4.9 11.5 1.0 HG3 A:ARG522 5.0 12.0 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