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Magnesium in PDB 5g20: Leishmania Major N-Myristoyltransferase in Complex with A Quinoline Inhibitor (Compound 19).

Enzymatic activity of Leishmania Major N-Myristoyltransferase in Complex with A Quinoline Inhibitor (Compound 19).

All present enzymatic activity of Leishmania Major N-Myristoyltransferase in Complex with A Quinoline Inhibitor (Compound 19).:
2.3.1.97;

Protein crystallography data

The structure of Leishmania Major N-Myristoyltransferase in Complex with A Quinoline Inhibitor (Compound 19)., PDB code: 5g20 was solved by V.Goncalves, J.A.Brannigan, A.Laporte, A.S.Bell, S.M.Roberts, A.J.Wilkinson, 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) 48.81 / 1.52
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 47.718, 90.651, 52.913, 90.00, 112.72, 90.00
R / Rfree (%) 17.4 / 21.9

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Leishmania Major N-Myristoyltransferase in Complex with A Quinoline Inhibitor (Compound 19). (pdb code 5g20). 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 Quinoline Inhibitor (Compound 19)., PDB code: 5g20:

Magnesium binding site 1 out of 1 in 5g20

Go back to Magnesium Binding Sites List in 5g20
Magnesium binding site 1 out of 1 in the Leishmania Major N-Myristoyltransferase in Complex with A Quinoline Inhibitor (Compound 19).


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 Quinoline Inhibitor (Compound 19). within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1422

b:27.5
occ:1.00
 O A:LEU175 2.7 22.7 1.0
O2A A:MYA1423 2.9 17.7 1.0
N A:LYS178 2.9 22.9 1.0
O4A A:MYA1423 3.0 17.9 1.0
N A:LEU180 3.1 18.5 1.0
N A:ARG179 3.4 21.1 1.0
N A:GLU177 3.4 24.3 1.0
CB A:LEU180 3.4 20.1 1.0
CA A:LYS178 3.5 25.4 1.0
C A:LYS178 3.6 22.9 1.0
CB A:LYS178 3.6 27.7 1.0
C A:ARG176 3.7 24.6 1.0
P1A A:MYA1423 3.7 19.1 1.0
CA A:LEU180 3.8 17.9 1.0
C A:LEU175 3.8 19.3 1.0
O1A A:MYA1423 3.9 20.4 1.0
CA A:ARG176 4.0 19.2 1.0
C A:GLU177 4.0 26.6 1.0
CG1 A:VAL171 4.0 18.6 1.0
C A:ARG179 4.1 23.0 1.0
CA A:GLU177 4.2 25.1 1.0
P2A A:MYA1423 4.2 18.5 1.0
CA A:ARG179 4.3 21.9 1.0
N A:ALA181 4.3 18.5 1.0
N A:ARG176 4.4 20.1 1.0
O3A A:MYA1423 4.4 18.2 1.0
O A:LYS178 4.4 22.7 1.0
O A:ARG176 4.5 24.4 1.0
C A:LEU180 4.5 19.2 1.0
CG A:LYS178 4.6 31.8 1.0
CG A:LEU180 4.7 23.3 1.0
O6A A:MYA1423 4.7 17.5 1.0
CG2 A:VAL171 4.7 18.7 1.0
CB A:VAL171 4.8 16.6 1.0
CD2 A:LEU180 5.0 22.2 1.0
CA A:LEU175 5.0 23.0 1.0

Reference:

V.Goncalves, J.A.Brannigan, A.Laporte, A.S.Bell, S.M.Roberts, A.J.Wilkinson, R.J.Leatherbarrow, E.W.Tate. Structure-Guided Optimization of Quinoline Inhibitors of Plasmodium N-Myristoyltransferase. Medchemcomm V. 8 191 2017.
ISSN: ISSN 2040-2503
PubMed: 28626547
DOI: 10.1039/C6MD00531D
Page generated: Sun Sep 29 04:34:45 2024

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