Zinc in PDB 8qhl: Human Angiotensin-1 Converting Enzyme N-Domain in Complex with the Lactotripeptide Vpp

All present enzymatic activity of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with the Lactotripeptide Vpp:
3.4.15.1;

The structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with the Lactotripeptide Vpp, PDB code: 8qhl was solved by K.S.Gregory, 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)	75.27 / 1.90
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	73.337, 78.222, 83.011, 88.75, 64.7, 75.25
R / Rfree (%)	18.8 / 23.3

The structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with the Lactotripeptide Vpp also contains other interesting chemical elements:

Chlorine	(Cl)	2 atoms
Magnesium	(Mg)	1 atom

The binding sites of Zinc atom in the Human Angiotensin-1 Converting Enzyme N-Domain in Complex with the Lactotripeptide Vpp (pdb code 8qhl). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Human Angiotensin-1 Converting Enzyme N-Domain in Complex with the Lactotripeptide Vpp, PDB code: 8qhl:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Human Angiotensin-1 Converting Enzyme N-Domain in Complex with the Lactotripeptide Vpp


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with the Lactotripeptide Vpp within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn701 b:25.2 occ:1.00 OE2 B:GLU389 2.0 23.7 1.0 NE2 B:HIS361 2.1 25.7 1.0 NE2 B:HIS365 2.1 21.6 1.0 N D:VAL52 2.1 23.4 1.0 O D:VAL52 2.3 28.1 1.0 C D:VAL52 2.9 25.2 1.0 CE1 B:HIS365 3.0 23.7 1.0 CE1 B:HIS361 3.0 26.9 1.0 CD B:GLU389 3.0 26.0 1.0 CD2 B:HIS361 3.1 27.8 1.0 CA D:VAL52 3.1 24.6 1.0 CD2 B:HIS365 3.2 22.6 1.0 OE1 B:GLU389 3.4 22.7 1.0 N D:PRO53 3.8 26.7 1.0 OE2 B:GLU362 3.9 27.1 1.0 CB D:VAL52 4.0 29.2 1.0 ND1 B:HIS361 4.2 23.4 1.0 ND1 B:HIS365 4.2 25.8 1.0 CG B:HIS361 4.2 25.7 1.0 O D:HOH103 4.3 31.3 1.0 CG B:HIS365 4.3 25.4 1.0 CG B:GLU389 4.4 21.3 1.0 CA D:PRO53 4.4 26.4 1.0 OH B:TYR501 4.5 22.8 1.0 CE1 B:TYR501 4.6 20.6 1.0 CA B:GLU389 4.6 23.2 1.0 O B:HOH961 4.7 25.6 1.0 CD B:GLU362 4.7 28.1 1.0 CB B:GLU389 4.8 26.4 1.0 CD D:PRO53 4.9 26.9 1.0 OE1 B:GLU362 4.9 26.0 1.0 CG2 D:VAL52 4.9 27.5 1.0

Zinc binding site 2 out of 2 in the Human Angiotensin-1 Converting Enzyme N-Domain in Complex with the Lactotripeptide Vpp


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with the Lactotripeptide Vpp within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn701 b:27.3 occ:1.00 OE2 A:GLU389 1.9 23.3 1.0 N C:VAL52 2.0 25.3 1.0 NE2 A:HIS361 2.1 23.6 1.0 NE2 A:HIS365 2.1 26.9 1.0 O C:VAL52 2.3 25.9 1.0 C C:VAL52 2.8 25.6 1.0 CD A:GLU389 2.9 27.8 1.0 CA C:VAL52 3.0 27.4 1.0 CD2 A:HIS361 3.1 22.6 1.0 CE1 A:HIS365 3.1 29.0 1.0 CE1 A:HIS361 3.1 24.2 1.0 CD2 A:HIS365 3.1 27.8 1.0 OE1 A:GLU389 3.3 26.4 1.0 N C:PRO53 3.8 28.4 1.0 CB C:VAL52 3.9 30.9 1.0 OE2 A:GLU362 3.9 28.6 1.0 ND1 A:HIS361 4.2 24.2 1.0 CG A:HIS361 4.2 23.3 1.0 ND1 A:HIS365 4.2 28.9 1.0 O A:HOH907 4.3 31.9 1.0 CG A:HIS365 4.3 30.1 1.0 CG A:GLU389 4.3 27.0 1.0 CA C:PRO53 4.4 31.2 1.0 OH A:TYR501 4.4 25.2 1.0 CE1 A:TYR501 4.6 25.7 1.0 O A:HOH895 4.6 22.5 1.0 CB A:GLU389 4.7 30.0 1.0 CD A:GLU362 4.7 29.5 1.0 CA A:GLU389 4.7 31.1 1.0 CG2 C:VAL52 4.7 24.1 1.0 OE1 A:GLU362 4.8 29.9 1.0 CD C:PRO53 4.8 27.3 1.0

K.S.Gregory, G.E.Cozier, S.L.U.Schwager, E.D.Sturrock, K.R.Acharya. Structural Insights Into the Inhibitory Mechanism of Angiotensin-I-Converting Enzyme By the Lactotripeptides Ipp and Vpp. Febs Lett. 2023.
ISSN: ISSN 0014-5793
PubMed: 37904282
DOI: 10.1002/1873-3468.14768