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Magnesium in PDB 5g21: Leishmania Major N-Myristoyltransferase in Complex with A Quinoline Inhibitor (Compound 26).

Enzymatic activity of Leishmania Major N-Myristoyltransferase in Complex with A Quinoline Inhibitor (Compound 26).

All present enzymatic activity of Leishmania Major N-Myristoyltransferase in Complex with A Quinoline Inhibitor (Compound 26).:
2.3.1.97;

Protein crystallography data

The structure of Leishmania Major N-Myristoyltransferase in Complex with A Quinoline Inhibitor (Compound 26)., PDB code: 5g21 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) 48.73 / 1.50
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 48.676, 91.068, 53.571, 90.00, 114.55, 90.00
R / Rfree (%) 17.4 / 20.9

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Leishmania Major N-Myristoyltransferase in Complex with A Quinoline Inhibitor (Compound 26). (pdb code 5g21). 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 26)., PDB code: 5g21:

Magnesium binding site 1 out of 1 in 5g21

Go back to Magnesium Binding Sites List in 5g21
Magnesium binding site 1 out of 1 in the Leishmania Major N-Myristoyltransferase in Complex with A Quinoline Inhibitor (Compound 26).


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 26). within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1000

b:29.4
occ:1.00
 O A:LEU175 2.6 23.6 1.0
O2A A:MYA1001 2.9 18.8 1.0
N A:LYS178 2.9 25.3 1.0
N A:LEU180 3.1 21.8 1.0
O4A A:MYA1001 3.1 18.6 1.0
N A:ARG179 3.3 23.0 1.0
CB A:LEU180 3.4 23.5 1.0
CA A:LYS178 3.5 21.1 1.0
C A:LYS178 3.5 23.5 1.0
N A:GLU177 3.5 22.8 1.0
CB A:LYS178 3.6 26.2 1.0
C A:ARG176 3.8 22.3 1.0
CA A:LEU180 3.8 24.2 1.0
C A:LEU175 3.8 23.1 1.0
P1A A:MYA1001 3.8 19.5 1.0
CA A:ARG176 3.9 22.6 1.0
O1A A:MYA1001 4.0 22.4 1.0
C A:GLU177 4.0 29.9 1.0
CG1 A:VAL171 4.1 18.3 1.0
C A:ARG179 4.1 23.3 1.0
CA A:GLU177 4.2 26.9 1.0
CA A:ARG179 4.2 22.3 1.0
P2A A:MYA1001 4.3 19.8 1.0
N A:ALA181 4.3 20.8 1.0
O A:LYS178 4.3 27.0 1.0
N A:ARG176 4.4 20.9 1.0
O3A A:MYA1001 4.4 19.3 1.0
CG A:LYS178 4.5 30.6 1.0
O A:ARG176 4.6 25.9 1.0
C A:LEU180 4.6 20.8 1.0
CG A:LEU180 4.7 22.8 1.0
CG2 A:VAL171 4.8 16.0 1.0
O6A A:MYA1001 4.8 17.3 1.0
CB A:VAL171 4.9 15.4 1.0
CA A:LEU175 5.0 24.8 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 04:34:53 2024

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