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Magnesium in PDB 6qdg: Leishmania Major N-Myristoyltransferase in Complex with Quinazoline Inhibitor Imp-0000169

Enzymatic activity of Leishmania Major N-Myristoyltransferase in Complex with Quinazoline Inhibitor Imp-0000169

All present enzymatic activity of Leishmania Major N-Myristoyltransferase in Complex with Quinazoline Inhibitor Imp-0000169:
2.3.1.97;

Protein crystallography data

The structure of Leishmania Major N-Myristoyltransferase in Complex with Quinazoline Inhibitor Imp-0000169, PDB code: 6qdg was solved by J.A.Brannigan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.75 / 1.98
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 48.598, 91.202, 53.344, 90.00, 113.96, 90.00
R / Rfree (%) 18.6 / 25.4

Other elements in 6qdg:

The structure of Leishmania Major N-Myristoyltransferase in Complex with Quinazoline Inhibitor Imp-0000169 also contains other interesting chemical elements:

Bromine (Br) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Leishmania Major N-Myristoyltransferase in Complex with Quinazoline Inhibitor Imp-0000169 (pdb code 6qdg). 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 Quinazoline Inhibitor Imp-0000169, PDB code: 6qdg:

Magnesium binding site 1 out of 1 in 6qdg

Go back to Magnesium Binding Sites List in 6qdg
Magnesium binding site 1 out of 1 in the Leishmania Major N-Myristoyltransferase in Complex with Quinazoline Inhibitor Imp-0000169


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 Quinazoline Inhibitor Imp-0000169 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1002

b:48.8
occ:1.00
 O A:LEU175 2.8 40.0 1.0
O1A A:MYA1001 2.8 36.0 1.0
O5A A:MYA1001 2.9 34.4 1.0
N A:LYS178 2.9 40.1 1.0
N A:LEU180 3.1 37.7 1.0
N A:GLU177 3.2 45.8 1.0
CB A:LEU180 3.4 35.7 1.0
N A:ARG179 3.4 44.0 1.0
C A:LYS178 3.5 44.2 1.0
CA A:LYS178 3.5 43.8 1.0
O2A A:MYA1001 3.7 46.5 1.0
P1A A:MYA1001 3.7 39.7 1.0
C A:ARG176 3.7 47.8 1.0
CA A:LEU180 3.8 37.6 1.0
CB A:LYS178 3.8 46.4 1.0
C A:LEU175 3.8 41.0 1.0
CA A:ARG176 3.9 40.2 1.0
C A:GLU177 3.9 47.4 1.0
CA A:GLU177 4.0 48.8 1.0
CG1 A:VAL171 4.0 32.5 1.0
P2A A:MYA1001 4.1 38.3 1.0
C A:ARG179 4.1 39.2 1.0
O A:LYS178 4.2 44.8 1.0
CA A:ARG179 4.2 43.6 1.0
N A:ARG176 4.3 38.0 1.0
O3A A:MYA1001 4.3 35.4 1.0
N A:ALA181 4.3 35.6 1.0
O A:ARG176 4.5 53.9 1.0
C A:LEU180 4.6 37.3 1.0
CG A:LYS178 4.6 50.7 1.0
CG A:LEU180 4.7 43.0 1.0
O6A A:MYA1001 4.7 34.5 1.0
CG2 A:VAL171 4.7 29.6 1.0
CB A:VAL171 4.8 31.8 1.0
CD2 A:LEU180 4.9 39.1 1.0

Reference:

J.A.Brannigan, J.A.Brannigan. N/A N/A.
Page generated: Wed Aug 13 14:45:13 2025

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