Chlorine in PDB 2xy9: Human Angiotensin Converting Enzyme in Complex with Phosphinic Tripeptide

All present enzymatic activity of Human Angiotensin Converting Enzyme in Complex with Phosphinic Tripeptide:
3.4.15.1;

The structure of Human Angiotensin Converting Enzyme in Complex with Phosphinic Tripeptide, PDB code: 2xy9 was solved by M.Akif, S.L.Schwager, C.S.Anthony, B.Czarny, F.Beau, V.Dive, E.D.Sturrock, K.R.Acharya, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.65 / 1.97
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	58.730, 86.094, 134.815, 90.00, 90.00, 90.00
R / Rfree (%)	19.889 / 23.18

The structure of Human Angiotensin Converting Enzyme in Complex with Phosphinic Tripeptide also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Chlorine atom in the Human Angiotensin Converting Enzyme in Complex with Phosphinic Tripeptide (pdb code 2xy9). 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 in Complex with Phosphinic Tripeptide, PDB code: 2xy9:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Human Angiotensin Converting Enzyme in Complex with Phosphinic Tripeptide


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 in Complex with Phosphinic Tripeptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1626 b:15.7 occ:1.00 NH2 A:ARG186 3.0 13.9 1.0 NE A:ARG186 3.1 14.6 1.0 NH2 A:ARG489 3.2 10.7 1.0 O A:HOH2365 3.2 15.1 1.0 NE1 A:TRP485 3.4 14.2 1.0 CZ A:ARG186 3.5 14.5 1.0 CZ2 A:TRP486 3.6 15.3 1.0 CZ A:ARG489 3.7 12.0 1.0 NE A:ARG489 3.7 12.4 1.0 CB A:ASP507 3.9 15.1 1.0 CH2 A:TRP486 4.0 14.9 1.0 CE2 A:TRP485 4.3 15.2 1.0 CD A:ARG186 4.3 15.4 1.0 CE2 A:TRP486 4.4 14.9 1.0 CD1 A:TRP485 4.4 14.5 1.0 CZ2 A:TRP485 4.4 15.5 1.0 CZ2 A:TRP182 4.5 14.5 1.0 O A:ASP507 4.6 14.9 1.0 CG A:ASP507 4.7 15.3 1.0 O A:HOH2231 4.8 10.2 1.0 C A:ASP507 4.8 14.5 1.0 NE1 A:TRP486 4.8 13.6 1.0 NH1 A:ARG489 4.8 10.4 1.0 NH1 A:ARG186 4.9 14.2 1.0 CA A:ASP507 4.9 15.2 1.0 CD A:ARG489 4.9 14.2 1.0 NE1 A:TRP182 5.0 14.8 1.0 CE2 A:TRP182 5.0 15.1 1.0

Chlorine binding site 2 out of 2 in the Human Angiotensin Converting Enzyme in Complex with Phosphinic Tripeptide


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 in Complex with Phosphinic Tripeptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1627 b:13.6 occ:1.00 OH A:TYR224 3.1 13.2 1.0 O A:HOH2178 3.1 12.2 1.0 NE A:ARG522 3.3 11.2 1.0 CB A:ARG522 3.5 11.0 1.0 CE1 A:TYR224 3.6 14.1 1.0 CB A:PRO519 3.6 11.6 1.0 N A:ARG522 3.6 10.8 1.0 NH2 A:ARG522 3.7 12.3 1.0 CAM A:3ES1636 3.8 18.1 1.0 CZ A:TYR224 3.8 13.2 1.0 CB A:PRO407 3.8 14.0 1.0 CG2 A:ILE521 4.0 10.0 1.0 CG A:PRO407 4.0 14.6 1.0 CAI A:3ES1636 4.0 18.2 1.0 CZ A:ARG522 4.0 11.8 1.0 CA A:ARG522 4.0 10.8 1.0 CG A:ARG522 4.0 10.8 1.0 CD A:ARG522 4.2 11.4 1.0 C A:PRO519 4.6 11.4 1.0 CG A:PRO519 4.6 11.7 1.0 C A:ILE521 4.6 10.5 1.0 O A:PRO519 4.7 11.6 1.0 N A:ILE521 4.7 10.2 1.0 CA A:PRO519 4.7 11.4 1.0 CD A:PRO407 4.9 14.1 1.0 CD1 A:TYR224 4.9 13.8 1.0 N A:TYR520 4.9 10.8 1.0 CA A:ILE521 5.0 10.6 1.0 CAS A:3ES1636 5.0 18.4 1.0

M.Akif, S.L.Schwager, C.S.Anthony, B.Czarny, F.Beau, V.Dive, E.D.Sturrock, K.R.Acharya. Novel Mechanism of Inhibition of Human Angiotensin- I-Converting Enzyme (Ace) By A Highly Specific Phosphinic Tripeptide. Biochem.J. V. 436 53 2011.
ISSN: ISSN 0264-6021
PubMed: 21352096
DOI: 10.1042/BJ20102123