Zinc in PDB 6f9r: Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Sampatrilat-Asp.

All present enzymatic activity of Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Sampatrilat-Asp.:
3.4.15.1;

The structure of Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Sampatrilat-Asp., PDB code: 6f9r was solved by G.E.Cozier, K.R.Acharya, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.39 / 1.85
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	72.591, 76.966, 82.637, 88.43, 64.40, 75.32
R / Rfree (%)	19.8 / 22.8

The structure of Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Sampatrilat-Asp. also contains other interesting chemical elements:

Magnesium	(Mg)	3 atoms
Chlorine	(Cl)	2 atoms

The binding sites of Zinc atom in the Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Sampatrilat-Asp. (pdb code 6f9r). 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 Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Sampatrilat-Asp., PDB code: 6f9r:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Sampatrilat-Asp.


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 Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Sampatrilat-Asp. within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn709 b:21.6 occ:1.00 OE1 A:GLU389 1.8 26.5 1.0 NE2 A:HIS361 1.9 25.0 1.0 NE2 A:HIS365 2.0 21.7 1.0 O38 A:D0W710 2.0 24.2 1.0 O37 A:D0W710 2.4 24.5 1.0 C36 A:D0W710 2.6 21.1 1.0 CE1 A:HIS365 2.8 30.1 1.0 CD A:GLU389 2.8 24.4 1.0 CE1 A:HIS361 2.9 23.6 1.0 HE1 A:HIS365 2.9 36.2 1.0 CD2 A:HIS361 3.0 23.3 1.0 CD2 A:HIS365 3.1 25.4 1.0 HE1 A:HIS361 3.1 28.4 1.0 HD2 A:HIS361 3.2 28.0 1.0 OE2 A:GLU389 3.2 24.7 1.0 HE1 A:TYR501 3.3 24.9 1.0 HD2 A:HIS365 3.3 30.5 1.0 HA A:GLU389 3.6 35.7 1.0 H202 A:D0W710 3.6 27.9 1.0 HH A:TYR501 3.7 27.4 1.0 H201 A:D0W710 3.7 27.9 1.0 H061 A:D0W710 3.9 59.4 1.0 ND1 A:HIS365 4.0 31.6 1.0 ND1 A:HIS361 4.0 23.9 1.0 CG A:HIS361 4.1 20.4 1.0 C14 A:D0W710 4.1 23.3 1.0 C20 A:D0W710 4.1 23.2 1.0 CG A:HIS365 4.1 27.7 1.0 CE1 A:TYR501 4.2 20.8 1.0 CG A:GLU389 4.2 25.8 1.0 HB3 A:GLU389 4.3 35.4 1.0 H141 A:D0W710 4.4 28.0 1.0 CA A:GLU389 4.4 29.8 1.0 OH A:TYR501 4.5 22.8 1.0 CB A:GLU389 4.5 29.5 1.0 HG3 A:GLU389 4.6 30.9 1.0 HD1 A:HIS365 4.7 37.9 1.0 OE2 A:GLU362 4.8 29.7 1.0 C06 A:D0W710 4.8 49.5 1.0 HD1 A:HIS361 4.8 28.7 1.0 HG2 A:GLU389 4.8 30.9 1.0 CZ A:TYR501 4.8 20.5 1.0 N12 A:D0W710 4.8 35.3 1.0 H062 A:D0W710 4.8 59.4 1.0 C15 A:D0W710 4.9 19.5 1.0 H151 A:D0W710 4.9 23.4 1.0 C10 A:D0W710 4.9 49.0 1.0 C13 A:D0W710 4.9 21.8 1.0 H271 A:D0W710 4.9 29.7 1.0 C16 A:D0W710 4.9 19.5 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Sampatrilat-Asp.


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 Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Sampatrilat-Asp. within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn710 b:28.1 occ:1.00 O38 B:D0W711 1.9 30.3 1.0 OE1 B:GLU389 1.9 34.2 1.0 NE2 B:HIS365 2.0 25.2 1.0 NE2 B:HIS361 2.1 28.3 1.0 C36 B:D0W711 2.5 30.6 1.0 O37 B:D0W711 2.5 27.2 1.0 CD B:GLU389 2.8 31.0 1.0 CD2 B:HIS365 3.0 25.5 1.0 CE1 B:HIS365 3.0 32.1 1.0 OE2 B:GLU389 3.0 33.5 1.0 CD2 B:HIS361 3.0 26.2 1.0 CE1 B:HIS361 3.1 25.3 1.0 HD2 B:HIS365 3.1 30.7 1.0 HE1 B:HIS365 3.2 38.6 1.0 HD2 B:HIS361 3.2 31.5 1.0 HE1 B:TYR501 3.2 29.0 1.0 HE1 B:HIS361 3.3 30.4 1.0 H202 B:D0W711 3.4 33.1 1.0 H201 B:D0W711 3.5 33.1 1.0 HH B:TYR501 3.5 34.5 1.0 HA B:GLU389 3.6 43.2 1.0 H061 B:D0W711 3.7 50.7 1.0 C20 B:D0W711 3.9 27.6 1.0 C14 B:D0W711 4.0 28.8 1.0 ND1 B:HIS365 4.1 32.9 1.0 CG B:HIS365 4.1 24.2 1.0 CE1 B:TYR501 4.1 24.2 1.0 CG B:GLU389 4.2 31.3 1.0 ND1 B:HIS361 4.2 22.2 1.0 CG B:HIS361 4.2 25.9 1.0 H141 B:D0W711 4.3 34.6 1.0 O B:HOH935 4.3 34.6 1.0 OH B:TYR501 4.3 28.7 1.0 HB3 B:GLU389 4.4 38.1 1.0 CA B:GLU389 4.4 36.0 1.0 H062 B:D0W711 4.5 50.7 1.0 CB B:GLU389 4.6 31.7 1.0 C06 B:D0W711 4.6 42.2 1.0 HG3 B:GLU389 4.6 37.6 1.0 N12 B:D0W711 4.7 34.0 1.0 OE2 B:GLU362 4.7 30.9 1.0 C16 B:D0W711 4.7 27.0 1.0 CZ B:TYR501 4.7 25.5 1.0 C15 B:D0W711 4.7 27.6 1.0 HG2 B:GLU389 4.8 37.6 1.0 H151 B:D0W711 4.8 33.1 1.0 C10 B:D0W711 4.8 46.7 1.0 C13 B:D0W711 4.8 26.9 1.0 HD1 B:HIS365 4.9 39.5 1.0 O11 B:D0W711 4.9 37.7 1.0 H271 B:D0W711 4.9 29.1 1.0 H121 B:D0W711 4.9 40.8 1.0 O B:HIS388 4.9 36.8 1.0 HD1 B:HIS361 5.0 26.6 1.0

G.E.Cozier, S.L.Schwager, R.K.Sharma, K.Chibale, E.D.Sturrock, K.R.Acharya. Crystal Structures of Sampatrilat and Sampatrilat-Asp in Complex with Human Ace - A Molecular Basis For Domain Selectivity. Febs J. V. 285 1477 2018.
ISSN: ISSN 1742-4658
PubMed: 29476645
DOI: 10.1111/FEBS.14421