Chlorine in PDB 4ca6: Human Angiotensin Converting Enzyme N-Domain in Complex with A Phosphinic Tripeptide Fi

All present enzymatic activity of Human Angiotensin Converting Enzyme N-Domain in Complex with A Phosphinic Tripeptide Fi:
3.4.15.1;

The structure of Human Angiotensin Converting Enzyme N-Domain in Complex with A Phosphinic Tripeptide Fi, PDB code: 4ca6 was solved by G.Masuyer, M.Akif, B.Czarny, F.Beau, S.L.U.Schwager, E.D.Sturrock, R.E.Isaac, V.Dive, K.R.Acharya, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.74 / 1.91
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	72.925, 76.643, 82.545, 88.62, 64.22, 75.58
R / Rfree (%)	18.675 / 22.296

The structure of Human Angiotensin Converting Enzyme N-Domain in Complex with A Phosphinic Tripeptide Fi also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Chlorine atom in the Human Angiotensin Converting Enzyme N-Domain in Complex with A Phosphinic Tripeptide Fi (pdb code 4ca6). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Human Angiotensin Converting Enzyme N-Domain in Complex with A Phosphinic Tripeptide Fi, PDB code: 4ca6:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Human Angiotensin Converting Enzyme N-Domain in Complex with A Phosphinic Tripeptide Fi


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Human Angiotensin Converting Enzyme N-Domain in Complex with A Phosphinic Tripeptide Fi within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1002 b:19.3 occ:1.00 OH A:TYR202 3.1 18.1 1.0 O A:HOH2120 3.1 20.9 1.0 NE A:ARG500 3.1 16.4 1.0 NH2 A:ARG500 3.5 15.7 1.0 CB A:ARG500 3.5 15.5 1.0 CB A:PRO497 3.6 16.9 1.0 CE1 A:TYR202 3.7 20.4 1.0 CZ A:ARG500 3.8 16.3 1.0 CB A:PRO385 3.8 19.1 1.0 CZ A:TYR202 3.8 19.8 1.0 N A:ARG500 3.8 15.3 1.0 CG A:PRO385 3.9 19.4 1.0 CE3 A:TRP201 4.0 35.7 1.0 CG A:ARG500 4.0 16.1 1.0 CA A:ARG500 4.1 15.7 1.0 CG2 A:ILE499 4.1 14.5 1.0 CD A:ARG500 4.2 16.3 1.0 CG A:PRO497 4.2 17.0 1.0 CZ3 A:TRP201 4.3 36.4 1.0 CD A:PRO385 4.7 19.6 1.0 C A:PRO497 4.8 16.2 1.0 CA A:PRO497 4.8 16.6 1.0 C A:ILE499 4.9 15.0 1.0 N A:ILE499 4.9 15.2 1.0 CD1 A:TYR202 5.0 20.9 1.0 O A:PRO497 5.0 15.7 1.0

Chlorine binding site 2 out of 2 in the Human Angiotensin Converting Enzyme N-Domain in Complex with A Phosphinic Tripeptide Fi


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Human Angiotensin Converting Enzyme N-Domain in Complex with A Phosphinic Tripeptide Fi within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1003 b:24.5 occ:1.00 OH B:TYR202 3.0 26.5 1.0 O B:HOH2096 3.0 29.4 1.0 NE B:ARG500 3.2 21.3 1.0 NH2 B:ARG500 3.5 21.2 1.0 CB B:ARG500 3.6 19.4 1.0 CB B:PRO497 3.6 19.7 1.0 CE1 B:TYR202 3.7 28.3 1.0 CZ B:ARG500 3.8 21.7 1.0 N B:ARG500 3.8 19.3 1.0 CZ B:TYR202 3.8 27.9 1.0 CB B:PRO385 3.8 24.3 1.0 CG B:PRO385 4.0 25.1 1.0 CG2 B:ILE499 4.0 19.9 1.0 CE3 B:TRP201 4.1 43.7 1.0 CG B:ARG500 4.1 20.1 1.0 CG B:PRO497 4.1 20.1 1.0 CA B:ARG500 4.1 19.0 1.0 CZ3 B:TRP201 4.2 43.2 1.0 CD B:ARG500 4.2 21.2 1.0 C B:ILE499 4.8 19.5 1.0 N B:ILE499 4.8 18.8 1.0 C B:PRO497 4.8 19.2 1.0 CD B:PRO385 4.8 25.7 1.0 CA B:PRO497 4.9 19.7 1.0 O B:HOH2200 4.9 23.8 1.0 CD1 B:TYR202 5.0 29.7 1.0 O B:PRO497 5.0 18.4 1.0

G.Masuyer, M.Akif, B.Czarny, F.Beau, S.L.Schwager, E.D.Sturrock, R.E.Isaac, V.Dive, K.R.Acharya. Crystal Structures of Highly Specific Phosphinic Tripeptide Enantiomers in Complex with the Angiotensin-I Converting Enzyme. Febs J. V. 281 943 2014.
ISSN: ISSN 1742-464X
PubMed: 24289879
DOI: 10.1111/FEBS.12660