Chlorine in PDB 2xyd: Human Angiotenisn Converting Enzyme N-Domain in Complex with Phosphinic Tripeptide

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

The structure of Human Angiotenisn Converting Enzyme N-Domain in Complex with Phosphinic Tripeptide, PDB code: 2xyd 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)	40.28 / 2.15
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	72.837, 76.437, 82.954, 89.11, 64.43, 75.87
R / Rfree (%)	21.991 / 25.589

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

Zinc

(Zn)

2 atoms

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

Chlorine binding site 1 out of 2 in the Human Angiotenisn Converting Enzyme N-Domain 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 Angiotenisn Converting Enzyme N-Domain in Complex with Phosphinic Tripeptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1621 b:23.8 occ:1.00 OH A:TYR202 2.9 29.4 1.0 O A:HOH2040 2.9 32.2 1.0 NE A:ARG500 3.2 19.1 1.0 NH2 A:ARG500 3.4 19.4 1.0 CB A:ARG500 3.6 19.0 1.0 CE2 A:TYR202 3.7 30.7 1.0 CB A:PRO497 3.7 24.0 1.0 CZ A:TYR202 3.7 30.1 1.0 CB A:PRO385 3.7 25.7 1.0 N A:ARG500 3.7 20.1 1.0 CZ A:ARG500 3.8 20.2 1.0 CG2 A:ILE499 3.9 19.9 1.0 CG A:PRO385 3.9 26.3 1.0 CA A:ARG500 4.1 19.7 1.0 CG A:ARG500 4.2 18.7 1.0 CE3 A:TRP201 4.2 38.8 1.0 CD A:ARG500 4.3 17.5 1.0 CG A:PRO497 4.4 25.1 1.0 CZ3 A:TRP201 4.5 39.4 1.0 C A:ILE499 4.8 20.6 1.0 N A:ILE499 4.8 21.7 1.0 CD A:PRO385 4.8 26.6 1.0 C A:PRO497 4.8 23.5 1.0 CA A:PRO497 4.9 23.9 1.0 CD2 A:TYR202 5.0 31.6 1.0

Chlorine binding site 2 out of 2 in the Human Angiotenisn Converting Enzyme N-Domain 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 Angiotenisn Converting Enzyme N-Domain in Complex with Phosphinic Tripeptide within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1620 b:31.6 occ:1.00 OH B:TYR202 3.0 42.0 1.0 O B:HOH2027 3.0 31.6 1.0 NE B:ARG500 3.2 25.3 1.0 NH2 B:ARG500 3.5 26.9 1.0 CB B:ARG500 3.6 23.8 1.0 CB B:PRO497 3.7 26.5 1.0 N B:ARG500 3.8 23.9 1.0 CZ B:ARG500 3.8 26.7 1.0 CE1 B:TYR202 3.8 42.3 1.0 CZ B:TYR202 3.8 42.4 1.0 CB B:PRO385 3.9 32.5 1.0 CE3 B:TRP201 4.0 45.7 1.0 CG2 B:ILE499 4.1 23.1 1.0 CG B:PRO385 4.1 33.1 1.0 CG B:ARG500 4.1 24.8 1.0 CZ3 B:TRP201 4.1 45.5 1.0 CA B:ARG500 4.1 23.9 1.0 CD B:ARG500 4.2 25.3 1.0 CG B:PRO497 4.3 26.5 1.0 C B:ILE499 4.7 24.1 1.0 N B:ILE499 4.7 24.2 1.0 C B:PRO497 4.8 26.0 1.0 O B:HOH2073 4.8 32.3 1.0 CA B:PRO497 4.9 26.3 1.0 CD B:PRO385 4.9 33.4 1.0 N B:TYR498 5.0 25.1 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