Zinc in PDB 6tt3: Crystal Structure of 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with SG6.

All present enzymatic activity of Crystal Structure of 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with SG6.:
3.4.15.1;

The structure of Crystal Structure of 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with SG6., PDB code: 6tt3 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)	75.11 / 1.70
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	73.617, 78.201, 83.789, 88.64, 64.35, 74.64
R / Rfree (%)	18.8 / 22.1

The structure of Crystal Structure of 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with SG6. also contains other interesting chemical elements:

Calcium	(Ca)	2 atoms
Chlorine	(Cl)	2 atoms

The binding sites of Zinc atom in the Crystal Structure of 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with SG6. (pdb code 6tt3). 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 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with SG6., PDB code: 6tt3:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with SG6.


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 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with SG6. within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn712 b:18.8 occ:1.00 NE2 A:HIS365 2.0 18.2 1.0 OE2 A:GLU389 2.0 20.0 1.0 O06 A:BJ2714 2.0 19.5 1.0 NE2 A:HIS361 2.1 17.7 1.0 O07 A:BJ2714 2.6 18.5 1.0 C05 A:BJ2714 2.6 20.9 1.0 CE1 A:HIS365 2.9 20.7 1.0 CD A:GLU389 2.9 17.4 1.0 HE1 A:HIS365 3.0 24.8 1.0 CE1 A:HIS361 3.0 17.4 1.0 CD2 A:HIS365 3.1 16.8 1.0 OE1 A:GLU389 3.1 19.3 1.0 CD2 A:HIS361 3.1 16.9 1.0 HE1 A:HIS361 3.2 20.9 1.0 HE1 A:TYR501 3.3 16.5 1.0 HD2 A:HIS361 3.3 20.4 1.0 HD2 A:HIS365 3.3 20.1 1.0 HA A:GLU389 3.6 22.1 1.0 H171 A:BJ2714 3.8 25.4 1.0 H021 A:BJ2714 3.8 25.1 1.0 HH A:TYR501 4.0 19.4 1.0 ND1 A:HIS365 4.0 20.0 1.0 H241 A:BJ2714 4.1 24.2 1.0 CE1 A:TYR501 4.1 13.8 1.0 C04 A:BJ2714 4.1 18.1 1.0 ND1 A:HIS361 4.2 15.7 1.0 CG A:HIS365 4.2 16.8 1.0 CG A:HIS361 4.2 17.9 1.0 CG A:GLU389 4.3 17.7 1.0 H041 A:BJ2714 4.4 21.8 1.0 OH A:TYR501 4.4 16.2 1.0 H172 A:BJ2714 4.4 25.4 1.0 CA A:GLU389 4.5 18.4 1.0 HB3 A:GLU389 4.5 21.7 1.0 C17 A:BJ2714 4.6 21.1 1.0 C02 A:BJ2714 4.7 20.9 1.0 CB A:GLU389 4.7 18.1 1.0 CZ A:TYR501 4.7 18.7 1.0 HG3 A:GLU389 4.8 21.3 1.0 O A:HOH1008 4.8 23.0 1.0 HD1 A:HIS365 4.8 24.0 1.0 H112 A:BJ2714 4.8 28.4 1.0 N12 A:BJ2714 4.8 17.1 1.0 OE2 A:GLU362 4.8 21.7 1.0 C13 A:BJ2714 4.8 22.9 1.0 HG2 A:GLU389 4.9 21.3 1.0 O14 A:BJ2714 4.9 23.2 1.0 N03 A:BJ2714 4.9 18.4 1.0 HD1 A:HIS361 4.9 18.8 1.0 C24 A:BJ2714 4.9 20.1 1.0 H252 A:BJ2714 5.0 25.0 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with SG6.


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 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with SG6. within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn708 b:23.7 occ:1.00 OE2 B:GLU389 1.8 22.7 1.0 O06 B:BJ2710 2.0 23.9 1.0 NE2 B:HIS365 2.1 29.9 1.0 NE2 B:HIS361 2.1 22.6 1.0 O07 B:BJ2710 2.4 26.3 1.0 C05 B:BJ2710 2.6 28.0 1.0 CD B:GLU389 2.8 23.9 1.0 CE1 B:HIS365 2.9 25.8 1.0 CD2 B:HIS361 3.0 19.5 1.0 CE1 B:HIS361 3.0 21.5 1.0 HE1 B:HIS365 3.0 30.9 1.0 OE1 B:GLU389 3.1 22.9 1.0 CD2 B:HIS365 3.1 27.6 1.0 HD2 B:HIS361 3.2 23.4 1.0 HE1 B:TYR501 3.2 22.9 1.0 HE1 B:HIS361 3.2 25.9 1.0 HD2 B:HIS365 3.4 33.2 1.0 HA B:GLU389 3.7 33.7 1.0 H171 B:BJ2710 3.8 39.6 1.0 HH B:TYR501 3.8 26.0 1.0 H021 B:BJ2710 3.8 30.9 1.0 H241 B:BJ2710 4.0 26.9 1.0 ND1 B:HIS365 4.1 28.9 1.0 C04 B:BJ2710 4.1 22.7 1.0 ND1 B:HIS361 4.1 23.1 1.0 CE1 B:TYR501 4.1 19.1 1.0 CG B:HIS361 4.1 17.3 1.0 CG B:GLU389 4.2 23.6 1.0 CG B:HIS365 4.2 26.2 1.0 H041 B:BJ2710 4.3 27.2 1.0 OH B:TYR501 4.4 21.6 1.0 HB3 B:GLU389 4.4 29.9 1.0 H172 B:BJ2710 4.4 39.6 1.0 CA B:GLU389 4.5 28.1 1.0 C17 B:BJ2710 4.5 33.0 1.0 HG3 B:GLU389 4.6 28.3 1.0 CB B:GLU389 4.6 24.9 1.0 C02 B:BJ2710 4.6 25.8 1.0 O B:HOH963 4.7 31.0 1.0 CZ B:TYR501 4.7 18.8 1.0 HG2 B:GLU389 4.8 28.3 1.0 C13 B:BJ2710 4.8 30.5 1.0 OE2 B:GLU362 4.8 27.0 1.0 O14 B:BJ2710 4.8 27.7 1.0 HD1 B:HIS365 4.8 34.7 1.0 HD1 B:HIS361 4.9 27.7 1.0 H112 B:BJ2710 4.9 35.1 1.0 N12 B:BJ2710 4.9 23.6 1.0 N03 B:BJ2710 4.9 20.8 1.0 C24 B:BJ2710 4.9 22.4 1.0

G.E.Cozier, L.Lubbe, E.D.Sturrock, K.R.Acharya. Ace-Domain Selectivity Extends Beyond Direct Interacting Residues at the Active Site. Biochem.J. 2020.
ISSN: ESSN 1470-8728
PubMed: 32195541
DOI: 10.1042/BCJ20200060