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Magnesium in PDB 6qdh: Leishmania Major N-Myristoyltransferase in Complex with Quinazoline Inhibitor Imp-0000906

Enzymatic activity of Leishmania Major N-Myristoyltransferase in Complex with Quinazoline Inhibitor Imp-0000906

All present enzymatic activity of Leishmania Major N-Myristoyltransferase in Complex with Quinazoline Inhibitor Imp-0000906:
2.3.1.97;

Protein crystallography data

The structure of Leishmania Major N-Myristoyltransferase in Complex with Quinazoline Inhibitor Imp-0000906, PDB code: 6qdh 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) 49.00 / 1.45
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 48.907, 91.592, 53.929, 90.00, 113.68, 90.00
R / Rfree (%) 18.7 / 22.2

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Leishmania Major N-Myristoyltransferase in Complex with Quinazoline Inhibitor Imp-0000906 (pdb code 6qdh). 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-0000906, PDB code: 6qdh:

Magnesium binding site 1 out of 1 in 6qdh

Go back to Magnesium Binding Sites List in 6qdh
Magnesium binding site 1 out of 1 in the Leishmania Major N-Myristoyltransferase in Complex with Quinazoline Inhibitor Imp-0000906


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-0000906 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1005

b:27.4
occ:1.00
O A:LEU175 2.7 21.8 1.0
N A:LYS178 2.9 23.3 1.0
O1A A:MYA1001 2.9 17.5 1.0
O5A A:MYA1001 3.1 20.3 1.0
N A:LEU180 3.1 20.8 1.0
N A:ARG179 3.3 22.2 1.0
N A:GLU177 3.4 21.8 1.0
CB A:LEU180 3.5 23.8 1.0
CA A:LYS178 3.5 23.6 1.0
C A:LYS178 3.5 22.9 1.0
CB A:LYS178 3.6 22.6 1.0
C A:ARG176 3.7 20.6 1.0
P1A A:MYA1001 3.8 18.1 1.0
C A:LEU175 3.8 21.7 1.0
O2A A:MYA1001 3.8 18.5 1.0
CA A:LEU180 3.8 23.8 1.0
CA A:ARG176 3.9 23.9 1.0
C A:GLU177 3.9 25.8 1.0
CG1 A:VAL171 4.1 18.4 1.0
C A:ARG179 4.1 24.2 1.0
CA A:GLU177 4.1 23.6 1.0
CA A:ARG179 4.2 22.8 1.0
P2A A:MYA1001 4.2 19.0 1.0
O A:LYS178 4.3 23.9 1.0
N A:ARG176 4.3 21.1 1.0
N A:ALA181 4.3 19.7 1.0
O3A A:MYA1001 4.4 18.3 1.0
CG A:LYS178 4.4 29.4 1.0
O A:ARG176 4.4 25.3 1.0
C A:LEU180 4.6 20.8 1.0
CG2 A:VAL171 4.8 18.1 1.0
O6A A:MYA1001 4.8 16.1 1.0
CG A:LEU180 4.8 23.6 1.0
CB A:VAL171 4.9 15.9 1.0
CA A:LEU175 5.0 21.0 1.0

Reference:

J.A.Brannigan, J.A.Brannigan. N/A N/A.
Page generated: Tue Oct 1 15:27:45 2024

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