Chlorine 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:

Zinc	(Zn)	2 atoms
Magnesium	(Mg)	1 atom

The binding sites of Chlorine 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 Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Human Angiotensin-1 Converting Enzyme N-Domain in Complex with the Lactotripeptide Vpp, PDB code: 8qhl:
Jump to Chlorine binding site number: 1; 2;

Chlorine 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 Chlorine with other atoms in the Cl 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:Cl702 b:24.8 occ:1.00 O B:HOH1013 3.0 25.9 1.0 OH B:TYR202 3.1 23.1 1.0 NE B:ARG500 3.3 23.1 1.0 NH2 B:ARG500 3.6 21.3 1.0 CB B:ARG500 3.6 21.9 1.0 CB B:PRO385 3.7 25.1 1.0 N B:ARG500 3.8 20.0 1.0 CB B:PRO497 3.8 21.3 1.0 CE1 B:TYR202 3.8 25.4 1.0 CZ3 B:TRP201 3.9 25.3 1.0 CG2 B:ILE499 3.9 18.5 1.0 CZ B:ARG500 3.9 23.4 1.0 CE3 B:TRP201 3.9 26.8 1.0 CZ B:TYR202 3.9 24.8 1.0 CG B:PRO385 4.0 21.0 1.0 CA B:ARG500 4.1 20.5 1.0 CG B:ARG500 4.2 21.2 1.0 CD B:ARG500 4.3 20.9 1.0 CG B:PRO497 4.6 21.9 1.0 N B:ILE499 4.8 19.7 1.0 CD B:PRO385 4.8 24.9 1.0 C B:ILE499 4.8 19.8 1.0 C B:PRO497 4.8 26.3 1.0 O B:HOH927 4.9 21.9 1.0 CA B:PRO497 4.9 21.2 1.0

Chlorine 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 Chlorine with other atoms in the Cl 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:Cl702 b:31.7 occ:1.00 O A:HOH954 3.0 32.3 1.0 OH A:TYR202 3.1 32.8 1.0 NE A:ARG500 3.2 26.3 1.0 NH2 A:ARG500 3.6 26.7 1.0 CB A:ARG500 3.7 27.9 1.0 CB A:PRO497 3.8 27.1 1.0 CE2 A:TYR202 3.8 32.7 1.0 CB A:PRO385 3.8 32.2 1.0 N A:ARG500 3.8 25.7 1.0 CZ A:TYR202 3.9 37.6 1.0 CZ A:ARG500 3.9 30.8 1.0 CG2 A:ILE499 3.9 25.1 1.0 CE3 A:TRP201 3.9 38.6 1.0 CZ3 A:TRP201 4.0 38.7 1.0 CG A:ARG500 4.0 28.8 1.0 CG A:PRO385 4.1 33.8 1.0 CA A:ARG500 4.2 29.3 1.0 CD A:ARG500 4.2 34.4 1.0 CG A:PRO497 4.6 29.3 1.0 CD A:PRO385 4.7 37.0 1.0 C A:ILE499 4.8 26.7 1.0 N A:ILE499 4.8 23.7 1.0 O A:HOH820 4.8 29.5 1.0 C A:PRO497 4.8 28.1 1.0 CA A:PRO497 5.0 25.1 1.0 N A:TYR498 5.0 24.8 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