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

Enzymatic activity of 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;

Protein crystallography data

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 / R_free (%)*	18.8 / 23.3

Other elements in 8qhl:

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
Zinc	(Zn)	2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium 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 Magnesium atom.
In total only one binding site of Magnesium was determined in the Human Angiotensin-1 Converting Enzyme N-Domain in Complex with the Lactotripeptide Vpp, PDB code: 8qhl:

Magnesium binding site 1 out of 1 in 8qhl

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Magnesium Binding Sites List in 8qhl

Magnesium binding site 1 out of 1 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 Magnesium with other atoms in the Mg 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
A:Mg706 b:49.2 occ:1.00	OE2	A:GLU262	2.0	43.8	1.0
	O	A:HOH875	2.3	49.7	1.0
	O	A:HOH865	2.3	39.2	1.0
	ND2	A:ASN263	3.0	33.1	1.0
	OD2	A:ASP354	3.0	67.4	1.0
	CD	A:GLU262	3.2	41.4	1.0
	CG	A:ASP354	3.5	65.1	1.0
	CG	A:GLU262	4.0	34.3	1.0
	CG	A:ASN263	4.0	37.0	1.0
	OD1	A:ASP354	4.0	62.3	1.0
	OE1	A:GLU262	4.1	38.1	1.0
	CB	A:ASP354	4.3	42.6	1.0
	OG	A:SER260	4.3	39.2	1.0
	O	A:HOH964	4.3	44.9	1.0
	OD1	A:ASN263	4.3	34.9	1.0
	O	A:HOH971	4.4	44.5	1.0
	O	A:HOH917	4.4	29.6	1.0
	O	A:HOH980	4.8	43.6	1.0
	OD2	A:ASP255	4.8	32.8	1.0

Reference:

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

Page generated: Fri Aug 15 13:08:57 2025

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