Zinc in PDB 6f9v: Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Sampatrilat.

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

The structure of Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Sampatrilat., PDB code: 6f9v 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)	21.97 / 1.69
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	73.224, 77.215, 83.107, 88.36, 64.20, 75.29
R / Rfree (%)	18.3 / 21.2

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

Magnesium	(Mg)	3 atoms
Chlorine	(Cl)	4 atoms

The binding sites of Zinc atom in the Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Sampatrilat. (pdb code 6f9v). 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., PDB code: 6f9v:
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.


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. within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn701 b:21.8 occ:1.00 NE2 A:HIS365 1.9 16.8 1.0 O39 A:D0Z702 1.9 21.6 1.0 OE1 A:GLU389 2.0 19.5 1.0 NE2 A:HIS361 2.0 18.4 1.0 O40 A:D0Z702 2.4 20.8 1.0 C38 A:D0Z702 2.6 25.6 1.0 CD A:GLU389 2.9 22.1 1.0 CE1 A:HIS365 2.9 21.5 1.0 CD2 A:HIS365 2.9 20.5 1.0 CE1 A:HIS361 3.0 19.5 1.0 CD2 A:HIS361 3.0 21.8 1.0 HE1 A:HIS365 3.1 25.8 1.0 HD2 A:HIS365 3.1 24.6 1.0 OE2 A:GLU389 3.1 21.6 1.0 HE1 A:HIS361 3.2 23.4 1.0 HD2 A:HIS361 3.2 26.2 1.0 HE1 A:TYR501 3.3 25.4 1.0 H222 A:D0Z702 3.5 28.0 1.0 HA A:GLU389 3.6 26.2 1.0 H221 A:D0Z702 3.6 28.0 1.0 H072 A:D0Z702 3.8 31.4 1.0 HH A:TYR501 3.8 27.2 1.0 ND1 A:HIS365 4.0 20.9 1.0 C22 A:D0Z702 4.0 23.4 1.0 CG A:HIS365 4.0 20.8 1.0 C16 A:D0Z702 4.1 24.3 1.0 ND1 A:HIS361 4.1 19.3 1.0 CG A:HIS361 4.1 17.7 1.0 CG A:GLU389 4.2 20.8 1.0 CE1 A:TYR501 4.2 21.2 1.0 H161 A:D0Z702 4.4 29.2 1.0 HB3 A:GLU389 4.4 28.2 1.0 CA A:GLU389 4.5 21.8 1.0 O A:HOH1072 4.5 25.1 1.0 H071 A:D0Z702 4.5 31.4 1.0 C07 A:D0Z702 4.6 26.1 1.0 OH A:TYR501 4.6 22.6 1.0 CB A:GLU389 4.6 23.5 1.0 HG3 A:GLU389 4.6 25.0 1.0 OE2 A:GLU362 4.7 27.0 1.0 N14 A:D0Z702 4.7 22.6 1.0 HD1 A:HIS365 4.7 25.1 1.0 H141 A:D0Z702 4.8 27.1 1.0 HG2 A:GLU389 4.8 25.0 1.0 C18 A:D0Z702 4.9 23.3 1.0 C17 A:D0Z702 4.9 22.0 1.0 HD1 A:HIS361 4.9 23.2 1.0 H331 A:D0Z702 4.9 31.1 1.0 C15 A:D0Z702 4.9 26.8 1.0 H171 A:D0Z702 4.9 26.4 1.0 CZ A:TYR501 4.9 21.4 1.0 C12 A:D0Z702 5.0 28.9 1.0 H091 A:D0Z702 5.0 41.5 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.


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. within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn701 b:22.5 occ:1.00 OE2 B:GLU389 1.9 25.0 1.0 O39 B:D0Z702 2.0 22.5 1.0 NE2 B:HIS365 2.0 21.6 1.0 NE2 B:HIS361 2.0 23.6 1.0 O40 B:D0Z702 2.5 24.1 1.0 C38 B:D0Z702 2.6 25.0 1.0 CD B:GLU389 2.9 21.3 1.0 CE1 B:HIS365 2.9 26.9 1.0 CE1 B:HIS361 3.0 20.9 1.0 HE1 B:HIS365 3.0 32.2 1.0 CD2 B:HIS361 3.0 21.4 1.0 CD2 B:HIS365 3.1 23.7 1.0 OE1 B:GLU389 3.1 25.2 1.0 HE1 B:HIS361 3.2 25.1 1.0 HD2 B:HIS361 3.3 25.6 1.0 HE1 B:TYR501 3.3 22.6 1.0 HD2 B:HIS365 3.3 28.4 1.0 H222 B:D0Z702 3.6 25.7 1.0 HA B:GLU389 3.6 36.9 1.0 HH B:TYR501 3.6 26.5 1.0 H221 B:D0Z702 3.6 25.7 1.0 H072 B:D0Z702 3.7 36.2 1.0 ND1 B:HIS365 4.1 27.0 1.0 C22 B:D0Z702 4.1 21.4 1.0 C16 B:D0Z702 4.1 22.8 1.0 ND1 B:HIS361 4.1 25.3 1.0 CG B:HIS361 4.2 20.7 1.0 CG B:HIS365 4.2 21.9 1.0 CE1 B:TYR501 4.2 18.9 1.0 H071 B:D0Z702 4.2 36.2 1.0 CG B:GLU389 4.3 25.6 1.0 H161 B:D0Z702 4.3 27.4 1.0 O B:HOH984 4.4 28.1 1.0 OH B:TYR501 4.4 22.1 1.0 HB3 B:GLU389 4.4 31.8 1.0 C07 B:D0Z702 4.4 30.2 1.0 CA B:GLU389 4.5 30.7 1.0 OE2 B:GLU362 4.5 27.7 1.0 CB B:GLU389 4.6 26.5 1.0 HG3 B:GLU389 4.7 30.7 1.0 N14 B:D0Z702 4.7 23.8 1.0 H141 B:D0Z702 4.7 28.6 1.0 CZ B:TYR501 4.8 20.0 1.0 HD1 B:HIS365 4.8 32.4 1.0 HG2 B:GLU389 4.8 30.7 1.0 HD1 B:HIS361 4.9 30.4 1.0 H331 B:D0Z702 4.9 28.9 1.0 C18 B:D0Z702 4.9 19.1 1.0 C17 B:D0Z702 4.9 21.4 1.0 C12 B:D0Z702 5.0 30.6 1.0 H171 B:D0Z702 5.0 25.7 1.0 C15 B:D0Z702 5.0 24.3 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