Magnesium in PDB 3wek: Crystal Structure of the Human Squalene Synthase F288L Mutant in Complex with Presqualene Pyrophosphate

Enzymatic activity of Crystal Structure of the Human Squalene Synthase F288L Mutant in Complex with Presqualene Pyrophosphate

All present enzymatic activity of Crystal Structure of the Human Squalene Synthase F288L Mutant in Complex with Presqualene Pyrophosphate:
2.5.1.21;

Protein crystallography data

The structure of Crystal Structure of the Human Squalene Synthase F288L Mutant in Complex with Presqualene Pyrophosphate, PDB code: 3wek was solved by C.I.Liu, W.Y.Jeng, A.H.J.Wang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	26.60 / 1.85
*Space group*	P 2₁ 2₁ 2
*Cell size a, b, c (Å), α, β, γ (°)*	94.192, 106.502, 32.988, 90.00, 90.00, 90.00
*R / R_free (%)*	22.5 / 25.7

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the Human Squalene Synthase F288L Mutant in Complex with Presqualene Pyrophosphate (pdb code 3wek). 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 the Human Squalene Synthase F288L Mutant in Complex with Presqualene Pyrophosphate, PDB code: 3wek:

Magnesium binding site 1 out of 1 in 3wek

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Magnesium Binding Sites List in 3wek

Magnesium binding site 1 out of 1 in the Crystal Structure of the Human Squalene Synthase F288L Mutant in Complex with Presqualene Pyrophosphate

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 the Human Squalene Synthase F288L Mutant in Complex with Presqualene Pyrophosphate within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Mg401 b:39.7 occ:1.00	O	A:HOH675	1.8	34.0	1.0
	OD1	A:ASP84	2.1	37.5	1.0
	OE1	A:GLU83	2.2	33.8	1.0
	O	A:HOH647	2.2	29.5	1.0
	O	A:HOH644	2.3	39.3	1.0
	OD1	A:ASP80	2.3	38.8	1.0
	CG	A:ASP84	3.0	34.9	1.0
	OD2	A:ASP84	3.2	37.5	1.0
	CG	A:ASP80	3.3	34.0	1.0
	CD	A:GLU83	3.4	34.0	1.0
	OD2	A:ASP80	3.5	38.0	1.0
	OE2	A:GLU83	4.1	33.2	1.0
	OH	A:TYR171	4.2	32.8	1.0
	O	A:ASP80	4.4	32.9	1.0
	CB	A:ASP84	4.4	36.2	1.0
	CB	A:GLU83	4.5	32.2	1.0
	CG	A:GLU83	4.5	33.5	1.0
	CB	A:ASP80	4.6	31.9	1.0
	N	A:ASP84	4.8	34.8	1.0
	CE	A:MET154	4.8	28.3	1.0
	CA	A:ASP84	4.9	36.2	1.0
	CA	A:ASP80	4.9	32.5	1.0

Reference:

C.I.Liu, W.Y.Jeng, W.J.Chang, M.F.Shih, T.P.Ko, A.H.J.Wang. Structural Insights Into the Catalytic Mechanism of Human Squalene Synthase Acta Crystallogr.,Sect.D V. 70 231 2014.
ISSN: ISSN 0907-4449
DOI: 10.1107/S1399004713026230

Page generated: Mon Aug 11 04:52:15 2025

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