Zinc in PDB 6tt1: Crystal Structure of 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with 33RE.

All present enzymatic activity of Crystal Structure of 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with 33RE.:
3.4.15.1;

The structure of Crystal Structure of 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with 33RE., PDB code: 6tt1 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)	44.59 / 1.80
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	73.166, 77.128, 82.867, 88.93, 64.53, 75.15
R / Rfree (%)	20 / 23.7

The structure of Crystal Structure of 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with 33RE. also contains other interesting chemical elements:

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 33RE. (pdb code 6tt1). 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 33RE., PDB code: 6tt1:
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 33RE.


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 33RE. within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn710 b:25.2 occ:1.00 NE2 A:HIS365 2.0 24.1 1.0 OE2 A:GLU389 2.0 22.7 1.0 NE2 A:HIS361 2.1 20.8 1.0 OAI A:1IU711 2.1 24.0 1.0 OAH A:1IU711 2.6 25.4 1.0 PBG A:1IU711 2.9 22.4 1.0 CE1 A:HIS365 2.9 24.2 1.0 CD A:GLU389 2.9 27.4 1.0 CD2 A:HIS365 3.0 24.2 1.0 CD2 A:HIS361 3.0 26.1 1.0 HE1 A:HIS365 3.0 29.1 1.0 CE1 A:HIS361 3.1 25.0 1.0 OE1 A:GLU389 3.1 24.1 1.0 HD2 A:HIS361 3.2 31.3 1.0 HE1 A:TYR501 3.2 23.7 1.0 HD2 A:HIS365 3.3 29.0 1.0 HE1 A:HIS361 3.3 30.0 1.0 HH A:TYR501 3.5 25.8 1.0 HA A:GLU389 3.7 28.2 1.0 ND1 A:HIS365 4.0 24.2 1.0 NAV A:1IU711 4.1 22.2 1.0 CE1 A:TYR501 4.1 19.8 1.0 CG A:HIS365 4.1 24.3 1.0 ND1 A:HIS361 4.2 21.7 1.0 CBC A:1IU711 4.2 23.0 1.0 CG A:HIS361 4.2 24.3 1.0 CBF A:1IU711 4.2 22.4 1.0 CAQ A:1IU711 4.3 23.3 1.0 CG A:GLU389 4.3 24.1 1.0 OH A:TYR501 4.3 21.5 1.0 HB3 A:GLU389 4.4 28.2 1.0 CAP A:1IU711 4.5 31.9 1.0 O A:HOH861 4.5 25.1 1.0 CA A:GLU389 4.6 23.5 1.0 CB A:GLU389 4.7 23.5 1.0 OE2 A:GLU362 4.7 25.9 1.0 CZ A:TYR501 4.7 22.5 1.0 CAZ A:1IU711 4.7 28.4 1.0 HG3 A:GLU389 4.8 28.9 1.0 HD1 A:HIS365 4.8 29.0 1.0 CAY A:1IU711 4.8 25.1 1.0 OE1 A:GLU362 4.8 24.7 1.0 HG2 A:GLU389 4.8 28.9 1.0 HD1 A:HIS361 4.9 26.0 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 33RE.


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 33RE. within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn707 b:25.9 occ:1.00 OE2 B:GLU389 1.9 28.6 1.0 NE2 B:HIS365 2.0 30.1 1.0 NE2 B:HIS361 2.0 25.0 1.0 OAI B:1IU708 2.2 22.3 1.0 OAH B:1IU708 2.6 26.4 1.0 CD B:GLU389 2.8 27.9 1.0 CE1 B:HIS365 2.9 29.0 1.0 PBG B:1IU708 2.9 24.1 1.0 CE1 B:HIS361 2.9 25.3 1.0 HE1 B:HIS365 3.0 34.8 1.0 OE1 B:GLU389 3.0 29.9 1.0 CD2 B:HIS361 3.0 26.3 1.0 HE1 B:HIS361 3.1 30.3 1.0 CD2 B:HIS365 3.1 29.6 1.0 HE1 B:TYR501 3.2 28.0 1.0 HD2 B:HIS361 3.3 31.5 1.0 HD2 B:HIS365 3.4 35.5 1.0 HH B:TYR501 3.6 27.6 1.0 HA B:GLU389 3.6 34.9 1.0 NAV B:1IU708 4.0 27.4 1.0 ND1 B:HIS361 4.0 25.6 1.0 ND1 B:HIS365 4.1 30.8 1.0 CE1 B:TYR501 4.1 23.4 1.0 CG B:HIS361 4.1 24.7 1.0 CBC B:1IU708 4.2 24.6 1.0 CG B:GLU389 4.2 27.7 1.0 CG B:HIS365 4.2 29.8 1.0 CBF B:1IU708 4.2 25.5 1.0 CAQ B:1IU708 4.2 24.3 1.0 OH B:TYR501 4.4 23.0 1.0 CAP B:1IU708 4.5 34.5 1.0 HB3 B:GLU389 4.5 33.1 1.0 O B:HOH943 4.5 27.8 1.0 CA B:GLU389 4.5 29.1 1.0 CB B:GLU389 4.6 27.6 1.0 HG3 B:GLU389 4.6 33.3 1.0 CZ B:TYR501 4.7 22.4 1.0 CAZ B:1IU708 4.8 31.1 1.0 HG2 B:GLU389 4.8 33.3 1.0 CAY B:1IU708 4.8 23.7 1.0 HD1 B:HIS361 4.8 30.8 1.0 HD1 B:HIS365 4.8 36.9 1.0 OE2 B:GLU362 4.9 23.7 1.0 OE1 B:GLU362 4.9 25.5 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