Magnesium in PDB 6h5x: Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Omapatrilat.

Enzymatic activity of Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Omapatrilat.

All present enzymatic activity of Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Omapatrilat.:
3.4.15.1;

Protein crystallography data

The structure of Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Omapatrilat., PDB code: 6h5x was solved by 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)*	44.60 / 1.80
*Space group*	P 1
*Cell size a, b, c (Å), α, β, γ (°)*	73.160, 76.953, 83.088, 88.83, 64.22, 75.21
*R / R_free (%)*	16.4 / 20.4

Other elements in 6h5x:

The structure of Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Omapatrilat. also contains other interesting chemical elements:

Zinc	(Zn)	2 atoms
Chlorine	(Cl)	2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Omapatrilat. (pdb code 6h5x). 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 Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Omapatrilat., PDB code: 6h5x:

Magnesium binding site 1 out of 1 in 6h5x

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Magnesium Binding Sites List in 6h5x

Magnesium binding site 1 out of 1 in the Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Omapatrilat.

Mono view

Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Omapatrilat. within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
B:Mg713 b:49.9 occ:1.00	OD1	B:ASN263	2.1	32.8	1.0
	O	B:HOH1044	2.4	42.2	1.0
	OE1	B:GLU262	2.5	39.0	0.6
	OE2	B:GLU262	2.6	38.3	0.6
	OD1	B:ASP354	2.6	39.9	1.0
	O	B:HOH965	2.8	57.2	1.0
	CD	B:GLU262	2.9	37.4	0.6
	O	B:HOH1156	3.1	55.7	1.0
	CG	B:ASN263	3.2	31.9	1.0
	HD21	B:ASN263	3.5	38.7	1.0
	CG	B:ASP354	3.6	39.2	1.0
	HB3	B:ASP354	3.7	39.8	1.0
	HG3	B:GLU262	3.7	40.1	0.4
	ND2	B:ASN263	3.7	32.2	1.0
	HB	B:THR352	3.8	35.7	1.0
	HA	B:ASN263	3.8	36.0	1.0
	H	B:ASP354	4.0	31.7	1.0
	HG1	B:THR352	4.2	35.8	1.0
	CB	B:ASP354	4.2	33.2	1.0
	O	B:HOH966	4.3	39.4	1.0
	CB	B:ASN263	4.4	30.9	1.0
	HB1	B:ALA148	4.4	40.4	1.0
	CG	B:GLU262	4.4	34.4	0.6
	OD2	B:ASP354	4.5	43.2	1.0
	HG21	B:THR352	4.5	35.6	1.0
	CA	B:ASN263	4.5	30.0	1.0
	HD22	B:ASN263	4.6	38.7	1.0
	CB	B:THR352	4.6	29.8	1.0
	CG	B:GLU262	4.6	33.4	0.4
	HG1	B:THR280	4.6	44.4	1.0
	OG1	B:THR352	4.6	29.8	1.0
	HG2	B:GLU262	4.8	40.1	0.4
	N	B:ASP354	4.8	26.4	1.0
	HG2	B:GLU262	4.8	41.3	0.6
	N	B:ASN263	4.8	28.6	1.0
	HG3	B:GLU262	4.8	41.3	0.6
	HB3	B:ASN263	4.8	37.0	1.0
	OG1	B:THR280	4.8	37.0	1.0
	HB2	B:GLU262	4.9	37.1	0.6
	HB2	B:ASP354	4.9	39.8	1.0
	O	B:HOH923	4.9	41.1	1.0
	OD2	B:ASP278	5.0	46.1	1.0

Reference:

G.E.Cozier, L.B.Arendse, S.L.Schwager, E.D.Sturrock, K.R.Acharya. Molecular Basis For Multiple Omapatrilat Binding Sites Within the Ace C-Domain: Implications For Drug Design. J. Med. Chem. V. 61 10141 2018.
ISSN: ISSN 1520-4804
PubMed: 30372620
DOI: 10.1021/ACS.JMEDCHEM.8B01309

Page generated: Tue Oct 1 01:33:21 2024

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