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

Go back to

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

Go back to

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

Go back to

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: Mon Aug 11 00:52:03 2025

Last articles

Mn in 9LJU
Mn in 9LJW
Mn in 9LJS
Mn in 9LJR
Mn in 9LJT
Mn in 9LJV
Mg in 9UA2
Mg in 9R96
Mg in 9VM1
Mg in 9P01

	© Copyright 2008-2020 by atomistry.com
Home \| Site Map \| Copyright \| Contact us \| Privacy