Zinc in PDB 6qs1: Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Bppb

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

The structure of Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Bppb, PDB code: 6qs1 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)	74.05 / 1.80
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	72.682, 77.070, 82.363, 88.86, 64.59, 75.03
R / Rfree (%)	20.2 / 23.2

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

Magnesium	(Mg)	2 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 Bppb (pdb code 6qs1). 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 Bppb, PDB code: 6qs1:
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 Bppb


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 Bppb within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn722 b:30.3 occ:0.70 NE2 A:HIS365 1.9 29.3 1.0 OE2 A:GLU389 1.9 26.9 1.0 NE2 A:HIS361 2.2 29.8 1.0 O E:ILE9 2.3 29.9 0.8 CE1 A:HIS365 2.8 29.7 1.0 CD A:GLU389 2.9 27.8 1.0 C E:ILE9 2.9 31.5 0.8 HE1 A:HIS365 2.9 35.7 1.0 CD2 A:HIS365 3.0 29.3 1.0 CD2 A:HIS361 3.0 30.6 1.0 H E:ILE9 3.0 47.1 0.8 HD2 A:HIS361 3.1 36.8 1.0 OE1 A:GLU389 3.2 29.3 1.0 HD2 A:HIS365 3.2 35.2 1.0 N E:ILE9 3.3 39.3 0.8 CE1 A:HIS361 3.3 28.2 1.0 HA E:PRO10 3.4 35.3 0.8 HE1 A:TYR501 3.5 28.7 1.0 HB3 E:LYS8 3.5 46.8 0.8 HE1 A:HIS361 3.6 33.9 1.0 CA E:ILE9 3.6 34.1 0.8 HA A:GLU389 3.7 31.3 1.0 N E:PRO10 3.7 31.5 0.8 HA E:ILE9 3.8 41.0 0.8 C E:LYS8 3.9 40.6 0.8 ND1 A:HIS365 3.9 29.4 1.0 HH A:TYR501 4.0 30.4 1.0 CA E:PRO10 4.0 29.4 0.8 OE2 A:GLU362 4.0 33.4 1.0 CG A:HIS365 4.0 27.4 1.0 O A:HOH901 4.2 29.0 1.0 CG A:HIS361 4.2 27.2 1.0 CG A:GLU389 4.3 25.1 1.0 ND1 A:HIS361 4.3 26.9 1.0 CE1 A:TYR501 4.3 23.9 1.0 CB E:LYS8 4.4 39.0 0.8 O E:LYS8 4.4 34.7 0.8 OH A:TYR501 4.5 25.3 1.0 HB3 A:GLU389 4.5 33.2 1.0 CA A:GLU389 4.5 26.1 1.0 CA E:LYS8 4.6 38.8 0.8 HA E:LYS8 4.6 46.6 0.8 HG3 A:GLU389 4.7 30.2 1.0 HD1 A:HIS365 4.7 35.3 1.0 CB A:GLU389 4.7 27.6 1.0 HB2 E:LYS8 4.7 46.8 0.8 HG12 E:ILE9 4.7 38.6 0.8 CD A:GLU362 4.8 32.9 1.0 HD2 E:LYS8 4.8 46.3 0.8 OE1 A:GLU362 4.8 31.9 1.0 HD3 E:PRO11 4.8 33.7 0.8 HD3 E:PRO10 4.9 39.9 0.8 HG2 A:GLU389 4.9 30.2 1.0 C E:PRO10 4.9 29.2 0.8 HG13 E:ILE9 4.9 38.6 0.8 CD E:PRO10 4.9 33.3 0.8 CZ A:TYR501 4.9 25.0 1.0 CB E:ILE9 5.0 34.4 0.8 HB3 E:PRO10 5.0 40.9 0.8

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


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 Bppb within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn714 b:29.5 occ:0.64 OE2 B:GLU389 1.9 28.9 1.0 NE2 B:HIS365 1.9 33.8 1.0 NE2 B:HIS361 2.1 31.1 1.0 O F:ILE9 2.2 31.5 0.9 C F:ILE9 2.7 34.9 0.9 CE1 B:HIS365 2.8 34.5 1.0 CD B:GLU389 2.9 30.7 1.0 HE1 B:HIS365 2.9 41.5 1.0 CD2 B:HIS361 2.9 32.5 1.0 H F:ILE9 3.0 51.8 0.9 HD2 B:HIS361 3.1 39.1 1.0 CD2 B:HIS365 3.1 32.8 1.0 N F:ILE9 3.1 43.1 0.9 CE1 B:HIS361 3.1 31.0 1.0 OE1 B:GLU389 3.2 32.7 1.0 HD2 B:HIS365 3.3 39.3 1.0 HA F:PRO10 3.3 40.6 0.9 CA F:ILE9 3.4 37.9 0.9 HE1 B:HIS361 3.4 37.3 1.0 HE1 B:TYR501 3.5 32.6 1.0 N F:PRO10 3.5 35.5 0.9 HA F:ILE9 3.6 45.5 0.9 HB3 F:LYS8 3.6 53.6 0.9 HA B:GLU389 3.8 38.5 1.0 OE2 B:GLU362 3.8 35.7 1.0 C F:LYS8 3.8 44.4 0.9 HH B:TYR501 3.8 32.3 1.0 CA F:PRO10 3.9 33.8 0.9 ND1 B:HIS365 4.0 34.4 1.0 CG B:HIS361 4.1 28.6 1.0 CG B:HIS365 4.1 34.3 1.0 ND1 B:HIS361 4.2 31.5 1.0 CG B:GLU389 4.3 30.6 1.0 O B:HOH887 4.3 32.9 1.0 O F:LYS8 4.3 41.4 0.9 CE1 B:TYR501 4.4 27.1 1.0 HB3 B:GLU389 4.4 39.4 1.0 CB F:LYS8 4.4 44.7 0.9 OH B:TYR501 4.4 26.9 1.0 CA F:LYS8 4.6 42.7 0.9 CA B:GLU389 4.6 32.0 1.0 HA F:LYS8 4.6 51.3 0.9 HG3 B:GLU389 4.7 36.8 1.0 CD B:GLU362 4.7 36.0 1.0 CB B:GLU389 4.7 32.8 1.0 HG12 F:ILE9 4.7 42.0 0.9 HD3 F:PRO10 4.7 39.9 0.9 HD1 B:HIS365 4.7 41.3 1.0 CD F:PRO10 4.7 33.2 0.9 HB2 F:LYS8 4.7 53.6 0.9 CB F:ILE9 4.8 38.9 0.9 C F:PRO10 4.8 32.1 0.9 OE1 B:GLU362 4.8 35.7 1.0 HG13 F:ILE9 4.9 42.0 0.9 HG2 B:GLU389 4.9 36.8 1.0 HD3 F:PRO11 4.9 38.5 0.9 CZ B:TYR501 4.9 26.8 1.0 HA B:GLU362 5.0 35.6 1.0 HD1 B:HIS361 5.0 37.9 1.0 HB3 F:PRO10 5.0 41.3 0.9

E.D.Sturrock, L.Lubbe, G.E.Cozier, S.L.U.Schwager, A.T.Arowolo, L.B.Arendse, E.Belcher, K.R.Acharya. Structural Basis For the C-Domain-Selective Angiotensin-Converting Enzyme Inhibition By Bradykinin-Potentiating Peptide B (Bppb). Biochem.J. V. 476 1553 2019.
ISSN: ESSN 1470-8728
PubMed: 31072910
DOI: 10.1042/BCJ20190290