Atomistry » Magnesium » PDB 5fux-5gg7 » 5g21
Atomistry »
  Magnesium »
    PDB 5fux-5gg7 »
      5g21 »

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: Mon Dec 14 20:20:16 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy