Magnesium in PDB 4cgn: Leishmania Major N-Myristoyltransferase in Complex with A Piperidinylindole Inhibitor

Enzymatic activity of Leishmania Major N-Myristoyltransferase in Complex with A Piperidinylindole Inhibitor

All present enzymatic activity of Leishmania Major N-Myristoyltransferase in Complex with A Piperidinylindole Inhibitor:
2.3.1.97;

Protein crystallography data

The structure of Leishmania Major N-Myristoyltransferase in Complex with A Piperidinylindole Inhibitor, PDB code: 4cgn was solved by J.A.Brannigan, S.M.Roberts, A.S.Bell, J.A.Hutton, D.F.Smith, E.W.Tate, R.J.Leatherbarrow, A.J.Wilkinson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	48.90 / 1.69
*Space group*	P 1 2₁ 1
*Cell size a, b, c (Å), α, β, γ (°)*	48.220, 91.280, 53.229, 90.00, 113.28, 90.00
*R / R_free (%)*	17.561 / 22.353

Other elements in 4cgn:

The structure of Leishmania Major N-Myristoyltransferase in Complex with A Piperidinylindole Inhibitor also contains other interesting chemical elements:

Fluorine

(F)

1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Leishmania Major N-Myristoyltransferase in Complex with A Piperidinylindole Inhibitor (pdb code 4cgn). 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 Leishmania Major N-Myristoyltransferase in Complex with A Piperidinylindole Inhibitor, PDB code: 4cgn:

Magnesium binding site 1 out of 1 in 4cgn

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Magnesium Binding Sites List in 4cgn

Magnesium binding site 1 out of 1 in the Leishmania Major N-Myristoyltransferase in Complex with A Piperidinylindole Inhibitor

Mono view

Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Leishmania Major N-Myristoyltransferase in Complex with A Piperidinylindole Inhibitor within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Mg999 b:23.9 occ:1.00	O	A:LEU175	2.7	19.5	1.0
	O2A	A:MYA1001	2.7	14.7	1.0
	N	A:LYS178	2.9	18.6	1.0
	O4A	A:MYA1001	3.0	15.7	1.0
	N	A:LEU180	3.1	16.2	1.0
	N	A:ARG179	3.4	19.2	1.0
	N	A:GLU177	3.4	16.8	1.0
	CB	A:LEU180	3.4	16.7	1.0
	CA	A:LYS178	3.4	19.6	1.0
	C	A:LYS178	3.5	20.3	1.0
	CB	A:LYS178	3.6	19.5	1.0
	P1A	A:MYA1001	3.7	17.8	1.0
	CA	A:LEU180	3.8	17.4	1.0
	C	A:ARG176	3.8	18.3	1.0
	C	A:LEU175	3.8	17.9	1.0
	O1A	A:MYA1001	3.8	17.6	1.0
	CA	A:ARG176	3.9	16.8	1.0
	C	A:GLU177	3.9	19.5	1.0
	CG1	A:VAL171	4.0	13.0	1.0
	C	A:ARG179	4.1	18.4	1.0
	CA	A:GLU177	4.1	17.3	1.0
	P2A	A:MYA1001	4.2	14.1	1.0
	CA	A:ARG179	4.2	18.9	1.0
	N	A:ALA181	4.3	16.0	1.0
	O	A:LYS178	4.3	22.6	1.0
	N	A:ARG176	4.3	17.4	1.0
	O3A	A:MYA1001	4.4	14.7	1.0
	CG	A:LYS178	4.5	24.5	1.0
	C	A:LEU180	4.6	17.2	1.0
	O	A:ARG176	4.6	18.8	1.0
	O6A	A:MYA1001	4.7	13.6	1.0
	CG	A:LEU180	4.7	19.7	1.0
	CG2	A:VAL171	4.8	13.5	1.0
	CB	A:VAL171	4.8	11.7	1.0
	CA	A:LEU175	5.0	18.9	0.5
	CA	A:LEU175	5.0	18.4	0.5

Reference:

J.A.Brannigan, S.M.Roberts, A.S.Bell, J.A.Hutton, M.R.Hodgkinson, E.W.Tate, R.J.Leatherbarrow, D.F.Smith, A.J.Wilkinson. Diverse Modes of Binding in Structures of Leishmania Major N-Myristoyltransferase with Selective Inhibitors Iucrj V. 1 250 2014.
ISSN: ISSN 2052-2525
PubMed: 25075346
DOI: 10.1107/S2052252514013001

Page generated: Thu Aug 15 16:48:07 2024

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