Zinc 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:

Chlorine

(Cl)

2 atoms

The binding sites of Zinc 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 Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Ac-Sd, PDB code: 4ufa:
Jump to Zinc binding site number: 1; 2;

Zinc 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 Zinc with other atoms in the Zn 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:Zn1001 b:17.7 occ:1.00 NE2 A:HIS365 2.0 15.6 1.0 OE1 A:GLU389 2.0 16.6 1.0 NE2 A:HIS361 2.0 14.8 1.0 O A:HOH2301 2.0 19.2 1.0 O A:HOH2300 2.4 25.8 1.0 CE1 A:HIS365 3.0 15.8 1.0 CD A:GLU389 3.0 16.4 1.0 CD2 A:HIS361 3.0 14.2 1.0 CD2 A:HIS365 3.0 15.3 1.0 CE1 A:HIS361 3.0 14.2 1.0 OE2 A:GLU389 3.2 16.1 1.0 CB A:SAC1301 4.0 49.1 1.0 ND1 A:HIS365 4.1 15.5 1.0 ND1 A:HIS361 4.1 14.2 1.0 CG A:HIS361 4.1 14.3 1.0 CG A:HIS365 4.2 15.0 1.0 CE1 A:TYR501 4.3 14.2 1.0 CG A:GLU389 4.4 16.6 1.0 OH A:TYR501 4.4 14.7 1.0 O A:HOH2283 4.4 30.0 1.0 O A:HOH2310 4.4 19.5 1.0 OE2 A:GLU362 4.5 19.8 1.0 OE1 A:GLU362 4.6 20.0 1.0 CA A:GLU389 4.7 16.1 1.0 CB A:GLU389 4.8 16.9 1.0 O A:SAC1301 4.8 50.2 1.0 CZ A:TYR501 4.8 14.9 1.0 CD A:GLU362 4.9 19.6 1.0 CA A:SAC1301 4.9 48.6 1.0 N A:SAC1301 4.9 51.3 1.0 OG A:SAC1301 4.9 49.7 1.0

Zinc 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 Zinc with other atoms in the Zn 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:Zn1001 b:17.8 occ:1.00 O B:HOH2234 2.0 19.1 1.0 NE2 B:HIS361 2.0 16.1 1.0 OE1 B:GLU389 2.0 18.8 1.0 NE2 B:HIS365 2.1 17.4 1.0 O B:HOH2235 2.1 27.4 1.0 CE1 B:HIS365 2.9 18.3 1.0 CE1 B:HIS361 2.9 15.5 1.0 CD2 B:HIS361 3.0 15.3 1.0 CD B:GLU389 3.0 19.4 1.0 CD2 B:HIS365 3.2 17.5 1.0 OE2 B:GLU389 3.2 18.8 1.0 ND1 B:HIS361 4.0 15.7 1.0 CB B:SAC1301 4.0 45.6 1.0 CG B:HIS361 4.1 15.3 1.0 ND1 B:HIS365 4.1 17.6 1.0 CE1 B:TYR501 4.2 16.4 1.0 CG B:HIS365 4.2 17.3 1.0 O B:HOH2216 4.3 34.0 1.0 OH B:TYR501 4.3 16.9 1.0 CG B:GLU389 4.4 19.6 1.0 OE2 B:GLU362 4.4 22.8 1.0 O B:HOH2242 4.4 21.2 1.0 C14 B:P6G1204 4.6 60.4 1.0 OE1 B:GLU362 4.7 23.1 1.0 CA B:GLU389 4.7 20.4 1.0 CZ B:TYR501 4.8 16.4 1.0 CB B:GLU389 4.8 20.4 1.0 CA B:SAC1301 4.8 45.9 1.0 O B:SAC1301 4.8 46.7 1.0 N B:SAC1301 4.9 49.8 1.0 CD B:GLU362 4.9 21.8 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