Magnesium in PDB 3nba: Phosphopantetheine Adenylyltranferase From Mycobacterium Tuberculosis in Complex with Adenosine-5'-[(Alpha,Beta)-Methyleno]Triphosphate (Ampcpp)

Enzymatic activity of Phosphopantetheine Adenylyltranferase From Mycobacterium Tuberculosis in Complex with Adenosine-5'-[(Alpha,Beta)-Methyleno]Triphosphate (Ampcpp)

All present enzymatic activity of Phosphopantetheine Adenylyltranferase From Mycobacterium Tuberculosis in Complex with Adenosine-5'-[(Alpha,Beta)-Methyleno]Triphosphate (Ampcpp):
2.7.7.3;

Protein crystallography data

The structure of Phosphopantetheine Adenylyltranferase From Mycobacterium Tuberculosis in Complex with Adenosine-5'-[(Alpha,Beta)-Methyleno]Triphosphate (Ampcpp), PDB code: 3nba was solved by T.J.Wubben, A.D.Mesecar, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	50.00 / 2.68
*Space group*	P 3 2 1
*Cell size a, b, c (Å), α, β, γ (°)*	115.118, 115.118, 133.913, 90.00, 90.00, 120.00
*R / R_free (%)*	19.9 / 25.6

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Phosphopantetheine Adenylyltranferase From Mycobacterium Tuberculosis in Complex with Adenosine-5'-[(Alpha,Beta)-Methyleno]Triphosphate (Ampcpp) (pdb code 3nba). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Phosphopantetheine Adenylyltranferase From Mycobacterium Tuberculosis in Complex with Adenosine-5'-[(Alpha,Beta)-Methyleno]Triphosphate (Ampcpp), PDB code: 3nba:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in 3nba

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Magnesium Binding Sites List in 3nba

Magnesium binding site 1 out of 3 in the Phosphopantetheine Adenylyltranferase From Mycobacterium Tuberculosis in Complex with Adenosine-5'-[(Alpha,Beta)-Methyleno]Triphosphate (Ampcpp)

Mono view

Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Phosphopantetheine Adenylyltranferase From Mycobacterium Tuberculosis in Complex with Adenosine-5'-[(Alpha,Beta)-Methyleno]Triphosphate (Ampcpp) within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Mg158 b:42.5 occ:1.00	O1G	A:APC200	2.5	59.6	1.0
	O2A	A:APC200	2.5	48.5	1.0
	O	A:HOH177	2.8	25.1	1.0
	C3A	A:APC200	3.3	49.9	1.0
	PA	A:APC200	3.5	47.7	1.0
	O	A:HOH256	3.7	38.3	1.0
	PG	A:APC200	3.7	59.5	1.0
	O3G	A:APC200	4.1	58.6	1.0
	PB	A:APC200	4.3	52.4	1.0
	O	A:HOH257	4.4	34.8	1.0
	O3B	A:APC200	4.4	56.9	1.0
	O1A	A:APC200	4.4	46.4	1.0
	O2B	A:APC200	4.4	53.2	1.0
	OG	A:SER9	4.5	18.5	0.5
	OG	A:SER9	4.5	18.3	0.5
	O5'	A:APC200	4.7	47.9	1.0
	CB	A:SER9	4.9	18.7	0.5
	O2G	A:APC200	4.9	59.4	1.0

Magnesium binding site 2 out of 3 in 3nba

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Magnesium Binding Sites List in 3nba

Magnesium binding site 2 out of 3 in the Phosphopantetheine Adenylyltranferase From Mycobacterium Tuberculosis in Complex with Adenosine-5'-[(Alpha,Beta)-Methyleno]Triphosphate (Ampcpp)

Mono view

Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Phosphopantetheine Adenylyltranferase From Mycobacterium Tuberculosis in Complex with Adenosine-5'-[(Alpha,Beta)-Methyleno]Triphosphate (Ampcpp) within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
C:Mg158 b:48.7 occ:1.00	O1G	C:APC200	2.4	61.5	1.0
	O2A	C:APC200	2.8	55.9	1.0
	C3A	C:APC200	3.3	56.1	1.0
	PA	C:APC200	3.6	55.6	1.0
	PG	C:APC200	3.8	59.1	1.0
	OG	C:SER9	4.0	28.0	1.0
	O3G	C:APC200	4.3	59.4	1.0
	O	C:HOH248	4.3	35.8	1.0
	PB	C:APC200	4.4	57.1	1.0
	O3B	C:APC200	4.6	59.8	1.0
	O2B	C:APC200	4.6	58.7	1.0
	O1A	C:APC200	4.6	54.0	1.0
	O	C:HOH249	4.9	34.3	1.0
	O5'	C:APC200	4.9	56.7	1.0
	O2G	C:APC200	4.9	58.6	1.0

Magnesium binding site 3 out of 3 in 3nba

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Magnesium Binding Sites List in 3nba

Magnesium binding site 3 out of 3 in the Phosphopantetheine Adenylyltranferase From Mycobacterium Tuberculosis in Complex with Adenosine-5'-[(Alpha,Beta)-Methyleno]Triphosphate (Ampcpp)

Mono view

Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Phosphopantetheine Adenylyltranferase From Mycobacterium Tuberculosis in Complex with Adenosine-5'-[(Alpha,Beta)-Methyleno]Triphosphate (Ampcpp) within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
D:Mg158 b:45.8 occ:1.00	O2A	D:APC200	2.5	63.2	1.0
	O1G	D:APC200	2.8	72.0	1.0
	C3A	D:APC200	3.0	64.7	1.0
	PA	D:APC200	3.4	61.4	1.0
	O	D:HOH265	4.0	33.6	1.0
	OG	D:SER9	4.1	31.9	1.0
	PG	D:APC200	4.2	70.3	1.0
	PB	D:APC200	4.3	68.1	1.0
	O1A	D:APC200	4.4	60.4	1.0
	O2B	D:APC200	4.5	67.6	1.0
	O5'	D:APC200	4.5	60.9	1.0
	O3B	D:APC200	4.7	69.7	1.0
	O2G	D:APC200	4.7	69.7	1.0
	O	D:HOH252	4.9	28.9	1.0

Reference:

T.J.Wubben, A.D.Mesecar. Kinetic, Thermodynamic, and Structural Insight Into the Mechanism of Phosphopantetheine Adenylyltransferase From Mycobacterium Tuberculosis. J.Mol.Biol. V. 404 202 2010.
ISSN: ISSN 0022-2836
PubMed: 20851704
DOI: 10.1016/J.JMB.2010.09.002

Page generated: Thu Aug 15 07:56:42 2024

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