Magnesium in PDB 5lqa: Rat Catechol O-Methyltransferase at High pH in Complex with A Bisubstrate Inhibitor

Enzymatic activity of Rat Catechol O-Methyltransferase at High pH in Complex with A Bisubstrate Inhibitor

All present enzymatic activity of Rat Catechol O-Methyltransferase at High pH in Complex with A Bisubstrate Inhibitor:
2.1.1.6;

Protein crystallography data

The structure of Rat Catechol O-Methyltransferase at High pH in Complex with A Bisubstrate Inhibitor, PDB code: 5lqa was solved by A.Ehler, M.Ellermann, M.G.Rudolph, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	31.01 / 1.20
*Space group*	P 2₁ 2₁ 2₁
*Cell size a, b, c (Å), α, β, γ (°)*	50.759, 56.352, 78.356, 90.00, 90.00, 90.00
*R / R_free (%)*	11.6 / 14.7

Other elements in 5lqa:

The structure of Rat Catechol O-Methyltransferase at High pH in Complex with A Bisubstrate Inhibitor also contains other interesting chemical elements:

Fluorine	(F)	1 atom
Chlorine	(Cl)	2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Rat Catechol O-Methyltransferase at High pH in Complex with A Bisubstrate Inhibitor (pdb code 5lqa). 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 Rat Catechol O-Methyltransferase at High pH in Complex with A Bisubstrate Inhibitor, PDB code: 5lqa:

Magnesium binding site 1 out of 1 in 5lqa

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Magnesium Binding Sites List in 5lqa

Magnesium binding site 1 out of 1 in the Rat Catechol O-Methyltransferase at High pH in Complex with A Bisubstrate Inhibitor

Mono view

Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Rat Catechol O-Methyltransferase at High pH in Complex with A Bisubstrate Inhibitor within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Mg305 b:6.8 occ:1.00	OD1	A:ASP141	2.1	7.1	1.0
	OD2	A:ASP169	2.1	7.5	1.0
	O	A:HOH428	2.1	8.2	1.0
	O34	A:619302	2.1	7.2	1.0
	OD1	A:ASN170	2.1	7.1	1.0
	O32	A:619302	2.1	7.0	1.0
	C33	A:619302	2.9	6.3	1.0
	C31	A:619302	2.9	6.6	1.0
	CG	A:ASP141	3.0	6.8	1.0
	CG	A:ASN170	3.1	6.6	1.0
	CG	A:ASP169	3.1	7.1	1.0
	OD2	A:ASP141	3.4	8.0	1.0
	ND2	A:ASN170	3.4	7.2	1.0
	CB	A:ASP169	3.7	6.4	1.0
	NZ	A:LYS144	3.8	6.9	1.0
	O	A:HOH532	3.8	18.1	1.0
	OD1	A:ASP169	4.2	7.8	1.0
	C23	A:619302	4.2	7.1	1.0
	OE2	A:GLU199	4.2	7.6	1.0
	C20	A:619302	4.3	7.1	1.0
	O	A:MET40	4.4	9.3	1.0
	CB	A:ASP141	4.4	6.7	1.0
	CB	A:ASN170	4.5	6.8	1.0
	O	A:ASP141	4.6	9.3	1.0
	CE	A:LYS144	4.7	7.1	1.0
	NZ	A:LYS46	4.7	7.6	1.0
	CG1	A:VAL42	4.8	7.7	0.3
	N17	A:619302	4.8	7.5	1.0
	CA	A:ASP141	4.8	6.2	1.0
	OE1	A:GLU199	4.8	8.1	1.0
	CD	A:GLU199	4.9	7.7	1.0

Reference:

M.Ellermann, M.G.Rudolph. Rat Catechol O-Methyltransferase at High pH in Complex with A Bisubstrate Inhibitor To Be Published.

Page generated: Tue Aug 12 14:38:52 2025

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