Magnesium in PDB 4myq: Selective Inhibition of the Catalytic Domain of Human Phosphodiesterase 4B with A-33

Enzymatic activity of Selective Inhibition of the Catalytic Domain of Human Phosphodiesterase 4B with A-33

All present enzymatic activity of Selective Inhibition of the Catalytic Domain of Human Phosphodiesterase 4B with A-33:
3.1.4.17;

Protein crystallography data

The structure of Selective Inhibition of the Catalytic Domain of Human Phosphodiesterase 4B with A-33, PDB code: 4myq was solved by D.Fox Iii, T.E.Edwards, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	49.85 / 1.90
*Space group*	P 4₂
*Cell size a, b, c (Å), α, β, γ (°)*	99.700, 99.700, 47.020, 90.00, 90.00, 90.00
*R / R_free (%)*	18.8 / 22.2

Other elements in 4myq:

The structure of Selective Inhibition of the Catalytic Domain of Human Phosphodiesterase 4B with A-33 also contains other interesting chemical elements:

Zinc	(Zn)	1 atom
Chlorine	(Cl)	1 atom
Sodium	(Na)	1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Selective Inhibition of the Catalytic Domain of Human Phosphodiesterase 4B with A-33 (pdb code 4myq). 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 Selective Inhibition of the Catalytic Domain of Human Phosphodiesterase 4B with A-33, PDB code: 4myq:

Magnesium binding site 1 out of 1 in 4myq

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Magnesium Binding Sites List in 4myq

Magnesium binding site 1 out of 1 in the Selective Inhibition of the Catalytic Domain of Human Phosphodiesterase 4B with A-33

Mono view

Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Selective Inhibition of the Catalytic Domain of Human Phosphodiesterase 4B with A-33 within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Mg702 b:9.3 occ:1.00	O	A:HOH840	2.2	8.3	1.0
	O	A:HOH950	2.2	17.3	1.0
	OD1	A:ASP447	2.2	6.4	1.0
	O	A:HOH817	2.2	6.4	1.0
	O	A:HOH844	2.2	6.7	1.0
	O	A:HOH969	2.3	10.7	1.0
	CG	A:ASP447	3.3	6.3	1.0
	OD2	A:ASP447	3.7	6.3	1.0
	ZN	A:ZN703	4.0	10.3	1.0
	OE2	A:GLU476	4.1	7.6	1.0
	NE2	A:HIS479	4.1	5.7	1.0
	O	A:HOH822	4.1	9.6	1.0
	O	A:HOH977	4.3	14.4	1.0
	CD2	A:HIS446	4.3	5.7	1.0
	O	A:HIS446	4.3	6.1	1.0
	O	A:HOH805	4.4	10.4	1.0
	CD2	A:HIS479	4.4	5.7	1.0
	CD2	A:HIS450	4.5	7.3	1.0
	OG1	A:THR517	4.5	8.2	1.0
	OD2	A:ASP564	4.5	7.4	1.0
	NE2	A:HIS406	4.5	7.5	1.0
	O	A:THR517	4.6	7.9	1.0
	CB	A:ASP447	4.6	6.2	1.0
	CD2	A:HIS406	4.6	7.4	1.0
	NE2	A:HIS446	4.7	5.6	1.0
	O	A:HOH877	4.7	14.0	1.0
	NE2	A:HIS450	4.8	7.3	1.0
	CA	A:ASP447	4.9	6.1	1.0
	CG	A:GLU476	5.0	7.0	1.0
	CD	A:GLU476	5.0	7.2	1.0

Reference:

D.Fox, A.B.Burgin, M.E.Gurney. Structural Basis For the Design of Selective Phosphodiesterase 4B Inhibitors. Cell Signal V. 26 657 2014.
PubMed: 24361374
DOI: 10.1016/J.CELLSIG.2013.12.003

Page generated: Mon Aug 11 20:34:05 2025

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