Chlorine in PDB 4ufa: Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Ac-Sd

All present enzymatic activity of Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Ac-Sd:
3.4.15.1;

The structure of Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Ac-Sd, PDB code: 4ufa was solved by G.Masuyer, R.G.Douglas, 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)	74.24 / 1.80
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	72.870, 76.720, 82.800, 88.65, 64.31, 75.22
R / Rfree (%)	20.232 / 22.822

The structure of Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Ac-Sd also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Chlorine atom in the Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Ac-Sd (pdb code 4ufa). 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 the Angiotensin-1 Converting Enzyme N- Domain in Complex with Ac-Sd, PDB code: 4ufa:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Ac-Sd


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 the Angiotensin-1 Converting Enzyme N- Domain in Complex with Ac-Sd within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1002 b:17.3 occ:1.00 OH A:TYR202 3.0 15.6 1.0 O A:HOH2166 3.0 18.3 1.0 NE A:ARG500 3.2 14.6 1.0 NH2 A:ARG500 3.5 13.6 1.0 CB A:ARG500 3.6 12.7 1.0 CB A:PRO385 3.7 15.0 1.0 CE2 A:TYR202 3.7 17.7 1.0 CB A:PRO497 3.7 13.6 1.0 N A:ARG500 3.8 12.4 1.0 CE3 A:TRP201 3.8 24.5 1.0 CZ A:TYR202 3.8 16.8 1.0 CZ3 A:TRP201 3.8 25.1 1.0 CZ A:ARG500 3.8 14.6 1.0 CG A:PRO385 3.8 15.0 1.0 CG2 A:ILE499 3.9 12.3 1.0 CG A:ARG500 4.1 13.2 1.0 CA A:ARG500 4.1 12.6 1.0 CD A:ARG500 4.3 14.4 1.0 CG A:PRO497 4.6 13.6 1.0 CD A:PRO385 4.7 15.1 1.0 C A:ILE499 4.7 12.5 1.0 N A:ILE499 4.8 13.2 1.0 C A:PRO497 4.8 14.0 1.0 O A:HOH2335 4.9 13.8 1.0 CA A:PRO497 4.9 13.6 1.0 CD2 A:TYR202 5.0 18.4 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Ac-Sd


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 the Angiotensin-1 Converting Enzyme N- Domain in Complex with Ac-Sd within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1002 b:21.0 occ:1.00 O B:HOH2125 3.0 25.6 1.0 OH B:TYR202 3.1 28.4 1.0 NE B:ARG500 3.2 19.1 1.0 NH2 B:ARG500 3.6 18.5 1.0 CB B:ARG500 3.6 17.2 1.0 CB B:PRO497 3.7 17.5 1.0 N B:ARG500 3.7 16.5 1.0 CE1 B:TYR202 3.7 28.8 1.0 CZ3 B:TRP201 3.8 30.2 1.0 CE3 B:TRP201 3.8 31.0 1.0 CZ B:TYR202 3.8 29.2 1.0 CB B:PRO385 3.9 24.1 1.0 CZ B:ARG500 3.9 19.6 1.0 CG2 B:ILE499 3.9 16.1 1.0 CG B:PRO385 4.0 24.7 1.0 CG B:ARG500 4.0 18.5 1.0 CA B:ARG500 4.1 16.9 1.0 CD B:ARG500 4.2 18.9 1.0 CG B:PRO497 4.5 17.5 1.0 N B:ILE499 4.7 15.9 1.0 CD B:PRO385 4.7 24.9 1.0 C B:ILE499 4.7 16.1 1.0 O B:HOH2261 4.8 22.3 1.0 C B:PRO497 4.8 17.2 1.0 CA B:PRO497 4.9 17.4 1.0 N B:TYR498 5.0 16.1 1.0 CA B:ILE499 5.0 15.8 1.0

G.Masuyer, R.G.Douglas, E.D.Sturrock, K.R.Acharya. Structural Basis of Ac-Sdkp Hydrolysis By Angiotensin-I Converting Enzyme Sci.Rep. V. 5 13742 2015.
ISSN: ISSN 2045-2322
PubMed: 26403559
DOI: 10.1038/SREP13742