Magnesium in PDB 4cyn: Leishmania Major N-Myristoyltransferase in Complex with An Aminoacylpyrrolidine Inhibitor (2B)

Enzymatic activity of Leishmania Major N-Myristoyltransferase in Complex with An Aminoacylpyrrolidine Inhibitor (2B)

All present enzymatic activity of Leishmania Major N-Myristoyltransferase in Complex with An Aminoacylpyrrolidine Inhibitor (2B):
2.3.1.97;

Protein crystallography data

The structure of Leishmania Major N-Myristoyltransferase in Complex with An Aminoacylpyrrolidine Inhibitor (2B), PDB code: 4cyn was solved by J.A.Hutton, V.Goncalves, J.A.Brannigan, D.Paape, T.Waugh, S.M.Roberts, A.S.Bell, A.J.Wilkinson, D.F.Smith, R.J.Leatherbarrow, E.W.Tate, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	49.35 / 1.40
*Space group*	P 1 2₁ 1
*Cell size a, b, c (Å), α, β, γ (°)*	47.668, 91.638, 53.163, 90.00, 111.82, 90.00
*R / R_free (%)*	17.418 / 21.226

Other elements in 4cyn:

The structure of Leishmania Major N-Myristoyltransferase in Complex with An Aminoacylpyrrolidine Inhibitor (2B) also contains other interesting chemical elements:

Chlorine

(Cl)

2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Leishmania Major N-Myristoyltransferase in Complex with An Aminoacylpyrrolidine Inhibitor (2B) (pdb code 4cyn). 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 An Aminoacylpyrrolidine Inhibitor (2B), PDB code: 4cyn:

Magnesium binding site 1 out of 1 in 4cyn

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Magnesium Binding Sites List in 4cyn

Magnesium binding site 1 out of 1 in the Leishmania Major N-Myristoyltransferase in Complex with An Aminoacylpyrrolidine Inhibitor (2B)

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 An Aminoacylpyrrolidine Inhibitor (2B) within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Mg999 b:21.3 occ:1.00	O	A:LEU175	2.7	15.8	1.0
	O2A	A:MYA1001	2.8	13.2	1.0
	N	A:LYS178	2.9	16.1	1.0
	O4A	A:MYA1001	3.0	11.8	1.0
	N	A:LEU180	3.1	13.9	1.0
	N	A:ARG179	3.3	15.0	1.0
	CB	A:LEU180	3.4	14.6	1.0
	N	A:GLU177	3.5	14.3	1.0
	CA	A:LYS178	3.5	16.3	1.0
	C	A:LYS178	3.5	16.4	1.0
	P1A	A:MYA1001	3.7	12.4	1.0
	CB	A:LYS178	3.7	16.6	1.0
	CA	A:LEU180	3.8	15.0	1.0
	C	A:ARG176	3.8	14.0	1.0
	C	A:LEU175	3.8	13.9	1.0
	O1A	A:MYA1001	3.9	13.6	1.0
	CG1	A:VAL171	4.0	11.8	1.0
	C	A:GLU177	4.0	16.4	1.0
	CA	A:ARG176	4.0	13.0	1.0
	C	A:ARG179	4.1	15.4	1.0
	CA	A:ARG179	4.1	14.3	1.0
	CA	A:GLU177	4.2	16.8	0.5
	CA	A:GLU177	4.2	16.6	0.5
	P2A	A:MYA1001	4.2	12.4	1.0
	N	A:ALA181	4.3	12.9	1.0
	O3A	A:MYA1001	4.3	12.4	1.0
	O	A:LYS178	4.4	18.6	1.0
	N	A:ARG176	4.4	13.4	1.0
	C	A:LEU180	4.6	14.0	1.0
	CG	A:LYS178	4.6	20.8	1.0
	O	A:ARG176	4.6	15.9	1.0
	O6A	A:MYA1001	4.7	11.2	1.0
	CG2	A:VAL171	4.8	11.3	1.0
	CG	A:LEU180	4.8	15.7	1.0
	CB	A:VAL171	4.8	9.8	1.0
	CD2	A:LEU180	5.0	16.6	1.0

Reference:

J.A.Hutton, V.Goncalves, J.A.Brannigan, D.Paape, M.H.Wright, T.M.Waugh, S.M.Roberts, A.S.Bell, A.J.Wilkinson, D.F.Smith, R.J.Leatherbarrow, E.W.Tate. Structure-Based Design of Potent and Selective Leishmania N- Myristoyltransferase Inhibitors. J.Med.Chem. V. 57 8664 2014.
ISSN: ISSN 0022-2623
PubMed: 25238611
DOI: 10.1021/JM5011397

Page generated: Mon Dec 14 11:42:07 2020

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