Magnesium 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
Chlorine	(Cl)	4 atoms

The binding sites of Magnesium 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 Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Human Angiotensin-1 Converting Enzyme N-Domain in Complex with the Lactotripeptide Ipp, PDB code: 8qfx:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium 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 Magnesium with other atoms in the Mg 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:Mg703 b:20.1 occ:1.00 OE2 A:GLU262 2.3 26.6 1.0 O A:HOH1238 2.3 31.2 1.0 O A:HOH920 2.3 25.0 1.0 OD2 A:ASP354 2.3 31.5 1.0 O A:HOH1262 2.6 28.9 1.0 OD1 A:ASN263 2.7 28.0 1.0 CD A:GLU262 3.4 23.2 1.0 CG A:ASP354 3.5 29.4 1.0 CG A:ASN263 3.8 22.0 1.0 ND2 A:ASN263 4.1 18.4 1.0 CG A:GLU262 4.1 20.5 1.0 CB A:ASP354 4.2 22.7 1.0 O A:HOH921 4.2 18.4 1.0 OE1 A:GLU262 4.2 20.8 1.0 O A:HOH1147 4.3 26.2 1.0 O A:HOH1305 4.3 22.8 1.0 OD1 A:ASP354 4.3 32.9 1.0 OG A:SER260 4.5 20.9 1.0 O A:HOH1302 4.5 26.1 1.0 OD1 A:ASP255 4.7 16.0 1.0 O A:HOH1105 4.8 27.4 1.0

Magnesium 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 Magnesium with other atoms in the Mg 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:Mg703 b:11.1 occ:1.00 O B:HOH1290 2.3 20.1 1.0 OD2 B:ASP354 2.3 21.9 1.0 OE2 B:GLU262 2.3 18.2 1.0 O B:HOH1002 2.4 19.1 1.0 O B:HOH1285 2.5 18.7 1.0 OD1 B:ASN263 2.5 19.6 1.0 CG B:ASP354 3.4 25.7 1.0 CG B:ASN263 3.5 16.4 1.0 CD B:GLU262 3.5 16.6 1.0 O B:HOH1119 3.8 35.3 1.0 ND2 B:ASN263 3.8 14.5 1.0 CB B:ASP354 4.2 18.1 1.0 O B:HOH920 4.2 14.3 1.0 CG B:GLU262 4.3 16.2 1.0 OD1 B:ASP354 4.3 26.0 1.0 O B:HOH1128 4.3 20.0 1.0 OE1 B:GLU262 4.4 12.9 1.0 O B:HOH1331 4.4 22.1 1.0 O B:HOH1346 4.5 21.2 1.0 OG B:SER260 4.6 15.5 1.0 OD1 B:ASP255 4.8 14.3 1.0 O B:HOH1127 4.8 12.9 1.0 CB B:ASN263 4.8 13.3 1.0 O B:HOH1035 4.9 24.7 1.0

Magnesium 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 Magnesium with other atoms in the Mg 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:Mg704 b:23.0 occ:1.00 OE2 C:GLU262 2.3 24.5 1.0 O C:HOH1014 2.3 32.5 1.0 OD2 C:ASP354 2.4 32.6 1.0 O C:HOH1252 2.4 33.0 1.0 O C:HOH1262 2.7 34.6 1.0 OD1 C:ASN263 2.8 26.7 1.0 CG C:ASP354 3.4 31.5 1.0 CD C:GLU262 3.4 24.8 1.0 CG C:ASN263 3.8 22.6 1.0 ND2 C:ASN263 4.1 20.1 1.0 CB C:ASP354 4.2 22.9 1.0 OD1 C:ASP354 4.2 35.0 1.0 O C:HOH1129 4.2 24.0 1.0 CG C:GLU262 4.2 21.2 1.0 OE1 C:GLU262 4.3 21.8 1.0 O C:HOH1300 4.3 27.4 1.0 O C:HOH952 4.3 16.1 1.0 OG C:SER260 4.4 22.4 1.0 O C:HOH1298 4.6 28.5 1.0 OD2 C:ASP255 4.8 19.5 1.0 O C:HOH1106 4.8 33.7 1.0

Magnesium 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 Magnesium with other atoms in the Mg 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:Mg704 b:29.5 occ:1.00 O D:HOH1139 2.2 32.9 1.0 OE2 D:GLU262 2.3 28.9 1.0 OD2 D:ASP354 2.4 43.0 1.0 O D:HOH1224 2.4 41.0 1.0 O D:HOH1245 2.8 32.5 1.0 OD1 D:ASN263 3.0 26.3 1.0 CD D:GLU262 3.5 30.1 1.0 CG D:ASP354 3.5 38.7 1.0 CG D:ASN263 3.9 24.9 1.0 O2 D:EDO710 4.1 31.1 1.0 ND2 D:ASN263 4.2 24.2 1.0 CB D:ASP354 4.2 30.4 1.0 CG D:GLU262 4.2 23.5 1.0 O D:HOH1274 4.2 26.0 1.0 OD1 D:ASP354 4.4 41.7 1.0 OE1 D:GLU262 4.4 24.5 1.0 O D:HOH961 4.4 20.6 1.0 O D:HOH1288 4.4 33.8 1.0 OG D:SER260 4.5 24.4 1.0 C1 D:EDO710 4.6 31.7 1.0 C2 D:EDO710 4.6 43.1 1.0 OD1 D:ASP255 4.8 20.2 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