Chlorine in PDB 8qfx: Human Angiotensin-1 Converting Enzyme N-Domain in Complex with the Lactotripeptide Ipp

The structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with the Lactotripeptide Ipp, PDB code: 8qfx was solved by K.S.Gregory, K.R.Acharya, G.E.Cozier, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	79.45 / 1.60
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	74.229, 103.395, 115.416, 84.95, 85.49, 81.55
R / Rfree (%)	18.1 / 21.1

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

Zinc	(Zn)	4 atoms
Magnesium	(Mg)	4 atoms

The binding sites of Chlorine atom in the Human Angiotensin-1 Converting Enzyme N-Domain in Complex with the Lactotripeptide Ipp (pdb code 8qfx). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Human Angiotensin-1 Converting Enzyme N-Domain in Complex with the Lactotripeptide Ipp, PDB code: 8qfx:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the Human Angiotensin-1 Converting Enzyme N-Domain in Complex with the Lactotripeptide Ipp


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 Ipp within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl702 b:15.6 occ:1.00 OH A:TYR202 3.1 17.0 1.0 NE A:ARG500 3.1 13.6 1.0 O A:HOH1133 3.2 14.8 1.0 NH2 A:ARG500 3.5 13.1 1.0 CB A:ARG500 3.7 13.2 1.0 CB A:PRO497 3.8 12.7 1.0 CB A:PRO385 3.8 14.5 1.0 CZ A:ARG500 3.8 14.4 1.0 CE2 A:TYR202 3.8 14.4 1.0 N A:ARG500 3.8 12.0 1.0 CZ A:TYR202 3.9 15.9 1.0 CG2 A:ILE499 4.0 12.4 1.0 CG A:PRO385 4.0 13.8 1.0 CE3 A:TRP201 4.0 19.8 1.0 CG A:ARG500 4.0 11.4 1.0 CZ3 A:TRP201 4.0 20.0 1.0 CA A:ARG500 4.2 12.8 1.0 CD A:ARG500 4.2 12.6 1.0 CD A:PRO385 4.7 13.2 1.0 C A:PRO497 4.7 11.7 1.0 CG A:PRO497 4.7 13.5 1.0 C A:ILE499 4.8 13.6 1.0 N A:ILE499 4.8 11.7 1.0 CA A:PRO497 4.9 11.9 1.0 O A:HOH990 5.0 15.2 1.0 O A:PRO497 5.0 11.4 1.0

Chlorine binding site 2 out of 4 in the Human Angiotensin-1 Converting Enzyme N-Domain in Complex with the Lactotripeptide Ipp


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 Ipp within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl702 b:14.3 occ:1.00 OH B:TYR202 3.1 13.7 1.0 O B:HOH1136 3.2 15.2 1.0 NE B:ARG500 3.3 11.9 1.0 NH2 B:ARG500 3.6 12.7 1.0 CB B:PRO385 3.6 13.5 1.0 CB B:ARG500 3.7 11.2 1.0 N B:ARG500 3.7 11.2 1.0 CB B:PRO497 3.7 11.8 1.0 CE2 B:TYR202 3.8 14.2 1.0 CZ B:TYR202 3.9 15.1 1.0 CZ B:ARG500 3.9 12.5 1.0 CE3 B:TRP201 3.9 16.6 1.0 CG B:PRO385 4.0 13.3 1.0 CG2 B:ILE499 4.0 12.9 1.0 CZ3 B:TRP201 4.0 15.8 1.0 CG B:ARG500 4.0 10.3 1.0 CA B:ARG500 4.1 11.1 1.0 CD B:ARG500 4.3 11.6 1.0 CG B:PRO497 4.7 12.6 1.0 N B:ILE499 4.7 10.3 1.0 CD B:PRO385 4.7 13.6 1.0 C B:ILE499 4.7 11.4 1.0 C B:PRO497 4.8 12.2 1.0 CA B:PRO497 4.9 11.0 1.0 O B:HOH1037 5.0 15.2 1.0

Chlorine binding site 3 out of 4 in the Human Angiotensin-1 Converting Enzyme N-Domain in Complex with the Lactotripeptide Ipp


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with the Lactotripeptide Ipp within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl703 b:14.6 occ:1.00 O C:HOH1177 3.1 15.9 1.0 OH C:TYR202 3.1 14.1 1.0 NE C:ARG500 3.2 11.4 1.0 NH2 C:ARG500 3.6 11.8 1.0 CB C:ARG500 3.7 12.1 1.0 CE2 C:TYR202 3.8 13.7 1.0 CB C:PRO497 3.8 10.9 1.0 N C:ARG500 3.8 12.3 1.0 CB C:PRO385 3.8 14.2 1.0 CZ C:ARG500 3.8 11.9 1.0 CZ C:TYR202 3.9 15.7 1.0 CG C:PRO385 4.0 14.5 1.0 CG2 C:ILE499 4.0 12.8 1.0 CE3 C:TRP201 4.0 17.4 1.0 CZ3 C:TRP201 4.0 16.4 1.0 CG C:ARG500 4.1 11.0 1.0 CA C:ARG500 4.2 12.4 1.0 CD C:ARG500 4.3 11.9 1.0 CG C:PRO497 4.7 11.4 1.0 N C:ILE499 4.8 11.3 1.0 CD C:PRO385 4.8 14.9 1.0 C C:ILE499 4.8 12.3 1.0 C C:PRO497 4.9 11.9 1.0 O C:HOH1080 4.9 13.6 1.0 CA C:PRO497 4.9 11.4 1.0

Chlorine binding site 4 out of 4 in the Human Angiotensin-1 Converting Enzyme N-Domain in Complex with the Lactotripeptide Ipp


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with the Lactotripeptide Ipp within 5.0Å range: probe atom residue distance (Å) B Occ D:Cl703 b:16.1 occ:1.00 OH D:TYR202 3.1 15.8 1.0 O D:HOH1173 3.2 15.9 1.0 NE D:ARG500 3.2 13.2 1.0 CB D:ARG500 3.6 15.6 1.0 NH2 D:ARG500 3.6 14.9 1.0 N D:ARG500 3.7 16.5 1.0 CB D:PRO385 3.7 16.0 1.0 CB D:PRO497 3.7 13.2 1.0 CE1 D:TYR202 3.8 16.4 1.0 CZ D:TYR202 3.9 17.3 1.0 CZ D:ARG500 3.9 13.7 1.0 CG2 D:ILE499 3.9 14.2 1.0 CG D:PRO385 4.0 16.9 1.0 CE3 D:TRP201 4.0 17.6 1.0 CZ3 D:TRP201 4.0 19.4 1.0 CG D:ARG500 4.1 14.0 1.0 CA D:ARG500 4.1 16.3 1.0 CD D:ARG500 4.2 14.1 1.0 CG D:PRO497 4.6 14.2 1.0 C D:ILE499 4.7 15.6 1.0 N D:ILE499 4.7 13.7 1.0 CD D:PRO385 4.8 17.3 1.0 C D:PRO497 4.8 15.1 1.0 O D:HOH979 4.8 16.4 1.0 CA D:PRO497 4.9 13.6 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