Zinc 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:

Magnesium	(Mg)	4 atoms
Chlorine	(Cl)	4 atoms

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

Zinc 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 Zinc with other atoms in the Zn 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:Zn701 b:14.4 occ:1.00 OE2 A:GLU389 2.0 13.3 1.0 NE2 A:HIS365 2.0 13.4 1.0 NE2 A:HIS361 2.1 12.2 1.0 N G:ILE1 2.1 17.0 1.0 O G:ILE1 2.3 13.2 1.0 C G:ILE1 2.9 13.4 1.0 CD A:GLU389 2.9 14.8 1.0 CE1 A:HIS361 3.0 12.7 1.0 CE1 A:HIS365 3.0 13.8 1.0 CD2 A:HIS365 3.1 13.4 1.0 CD2 A:HIS361 3.1 11.5 1.0 CA G:ILE1 3.1 13.7 1.0 OE1 A:GLU389 3.2 16.8 1.0 N G:PRO2 3.9 14.4 1.0 CB G:ILE1 3.9 13.4 1.0 OE2 A:GLU362 4.0 15.7 1.0 O4 A:PGE704 4.1 51.5 1.0 ND1 A:HIS361 4.2 13.6 1.0 ND1 A:HIS365 4.2 13.8 1.0 CG A:HIS361 4.2 12.0 1.0 CG A:HIS365 4.2 13.3 1.0 CG A:GLU389 4.3 14.1 1.0 O A:HOH1058 4.4 18.1 1.0 CA G:PRO2 4.4 14.9 1.0 OH A:TYR501 4.5 11.1 1.0 CA A:GLU389 4.6 14.3 1.0 CE1 A:TYR501 4.6 11.7 1.0 CB A:GLU389 4.7 15.5 1.0 O A:HOH988 4.7 16.2 1.0 CD A:GLU362 4.7 15.7 1.0 CG1 G:ILE1 4.8 14.8 1.0 OE1 A:GLU362 4.8 14.7 1.0 CD G:PRO2 4.9 14.5 1.0

Zinc 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 Zinc with other atoms in the Zn 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:Zn701 b:12.9 occ:1.00 OE2 B:GLU389 2.0 13.8 1.0 NE2 B:HIS365 2.1 12.4 1.0 NE2 B:HIS361 2.1 13.2 1.0 N F:ILE1 2.1 13.5 1.0 O F:ILE1 2.5 11.6 1.0 C F:ILE1 2.9 11.9 1.0 CD B:GLU389 2.9 14.0 1.0 CE1 B:HIS361 3.0 13.2 1.0 CD2 B:HIS365 3.0 12.2 1.0 CA F:ILE1 3.1 12.9 1.0 CE1 B:HIS365 3.1 12.5 1.0 CD2 B:HIS361 3.1 11.9 1.0 OE1 B:GLU389 3.2 14.9 1.0 N F:PRO2 3.8 13.6 1.0 OE2 B:GLU362 3.9 15.3 1.0 CB F:ILE1 3.9 15.2 1.0 ND1 B:HIS361 4.1 11.9 1.0 ND1 B:HIS365 4.2 12.3 1.0 CG B:HIS365 4.2 12.5 1.0 CG B:HIS361 4.2 12.2 1.0 CG B:GLU389 4.3 12.9 1.0 CA F:PRO2 4.4 13.4 1.0 O B:HOH1082 4.4 17.4 1.0 OH B:TYR501 4.5 10.8 1.0 CA B:GLU389 4.6 13.0 1.0 CE1 B:TYR501 4.6 11.1 1.0 O1 B:PEG706 4.6 46.6 1.0 O B:HOH1086 4.7 15.1 1.0 CD B:GLU362 4.7 15.1 1.0 CB B:GLU389 4.7 12.8 1.0 CD F:PRO2 4.9 14.0 1.0 OE1 B:GLU362 4.9 14.6 1.0 CG1 F:ILE1 4.9 16.8 1.0

Zinc 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 Zinc with other atoms in the Zn 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:Zn702 b:13.6 occ:1.00 OE2 C:GLU389 1.9 14.4 1.0 N E:ILE1 2.1 14.5 1.0 NE2 C:HIS361 2.1 11.2 1.0 NE2 C:HIS365 2.2 12.6 1.0 O E:ILE1 2.4 12.0 1.0 CD C:GLU389 2.9 14.3 1.0 C E:ILE1 2.9 13.7 1.0 CE1 C:HIS361 3.0 11.3 1.0 CA E:ILE1 3.1 13.4 1.0 CD2 C:HIS361 3.1 12.3 1.0 CD2 C:HIS365 3.2 13.0 1.0 CE1 C:HIS365 3.2 12.8 1.0 OE1 C:GLU389 3.3 14.3 1.0 N E:PRO2 3.8 11.7 1.0 OE2 C:GLU362 3.9 13.4 1.0 CB E:ILE1 3.9 13.7 1.0 ND1 C:HIS361 4.1 11.3 1.0 CG C:HIS361 4.2 11.2 1.0 ND1 C:HIS365 4.3 12.2 1.0 CG C:GLU389 4.3 12.7 1.0 CG C:HIS365 4.3 11.4 1.0 O C:HOH1082 4.4 15.5 1.0 CA E:PRO2 4.4 13.5 1.0 OH C:TYR501 4.5 12.8 1.0 CA C:GLU389 4.6 13.6 1.0 CE1 C:TYR501 4.6 11.7 1.0 CB C:GLU389 4.6 13.7 1.0 O C:HOH915 4.6 14.9 1.0 CD C:GLU362 4.7 14.2 1.0 CG1 E:ILE1 4.8 13.7 1.0 OE1 C:GLU362 4.8 14.0 1.0 CD E:PRO2 4.9 13.0 1.0

Zinc 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 Zinc with other atoms in the Zn 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:Zn702 b:16.3 occ:1.00 OE2 D:GLU389 2.0 16.1 1.0 NE2 D:HIS365 2.1 14.7 1.0 NE2 D:HIS361 2.1 14.6 1.0 N H:ILE1 2.1 16.3 1.0 O H:ILE1 2.5 13.7 1.0 C H:ILE1 2.9 16.3 1.0 CD D:GLU389 2.9 15.8 1.0 CE1 D:HIS361 3.0 15.1 1.0 CE1 D:HIS365 3.0 15.9 1.0 CA H:ILE1 3.1 17.4 1.0 CD2 D:HIS365 3.1 15.2 1.0 CD2 D:HIS361 3.1 15.1 1.0 OE1 D:GLU389 3.3 16.3 1.0 N H:PRO2 3.9 15.3 1.0 OE2 D:GLU362 3.9 16.2 1.0 CB H:ILE1 3.9 13.3 1.0 ND1 D:HIS361 4.1 16.0 1.0 ND1 D:HIS365 4.2 16.9 1.0 CG D:HIS361 4.2 15.3 1.0 CG D:HIS365 4.2 15.4 1.0 CG D:GLU389 4.3 14.1 1.0 O D:HOH1092 4.4 17.5 1.0 CA H:PRO2 4.5 16.2 1.0 OH D:TYR501 4.5 16.2 1.0 CE1 D:TYR501 4.5 15.6 1.0 CA D:GLU389 4.6 15.5 1.0 CB D:GLU389 4.6 14.6 1.0 O D:HOH1004 4.7 17.1 1.0 CD D:GLU362 4.7 16.9 1.0 CG1 H:ILE1 4.8 17.2 1.0 OE1 D:GLU362 4.9 17.6 1.0 CD H:PRO2 4.9 14.5 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