Atomistry » Magnesium » PDB 6q5a-6qin » 6qde
Atomistry »
  Magnesium »
    PDB 6q5a-6qin »
      6qde »

Magnesium in PDB 6qde: Leishmania Major N-Myristoyltransferase in Complex with Thienopyrimidine Inhibitor Imp-0000877

Enzymatic activity of Leishmania Major N-Myristoyltransferase in Complex with Thienopyrimidine Inhibitor Imp-0000877

All present enzymatic activity of Leishmania Major N-Myristoyltransferase in Complex with Thienopyrimidine Inhibitor Imp-0000877:
2.3.1.97;

Protein crystallography data

The structure of Leishmania Major N-Myristoyltransferase in Complex with Thienopyrimidine Inhibitor Imp-0000877, PDB code: 6qde 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) 45.00 / 1.45
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 47.874, 90.474, 53.268, 90.00, 111.72, 90.00
R / Rfree (%) 16.1 / 19.6

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Leishmania Major N-Myristoyltransferase in Complex with Thienopyrimidine Inhibitor Imp-0000877 (pdb code 6qde). 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 Thienopyrimidine Inhibitor Imp-0000877, PDB code: 6qde:

Magnesium binding site 1 out of 1 in 6qde

Go back to Magnesium Binding Sites List in 6qde
Magnesium binding site 1 out of 1 in the Leishmania Major N-Myristoyltransferase in Complex with Thienopyrimidine Inhibitor Imp-0000877


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 Thienopyrimidine Inhibitor Imp-0000877 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg501

b:18.1
occ:1.00
 O A:LEU175 2.7 10.9 1.0
O1A A:MYA504 2.9 8.5 1.0
N A:LYS178 2.9 11.2 1.0
N A:LEU180 3.1 8.5 1.0
O5A A:MYA504 3.1 8.2 1.0
N A:ARG179 3.3 9.3 1.0
N A:GLU177 3.4 10.3 1.0
CA A:LYS178 3.5 11.3 1.0
CB A:LEU180 3.5 8.5 1.0
C A:LYS178 3.5 11.0 1.0
P1A A:MYA504 3.7 8.2 1.0
CB A:LYS178 3.7 13.6 1.0
O2A A:MYA504 3.7 8.7 1.0
C A:ARG176 3.8 10.3 1.0
C A:LEU175 3.8 11.0 1.0
CA A:LEU180 3.9 8.0 1.0
C A:GLU177 3.9 12.9 1.0
CA A:ARG176 4.0 10.1 1.0
C A:ARG179 4.1 9.5 1.0
CG1 A:VAL171 4.1 7.7 1.0
CA A:GLU177 4.1 12.8 1.0
CA A:ARG179 4.2 9.4 1.0
P2A A:MYA504 4.2 8.7 1.0
N A:ALA181 4.3 7.9 1.0
O A:LYS178 4.3 11.3 1.0
O3A A:MYA504 4.4 8.8 1.0
N A:ARG176 4.4 9.9 1.0
CG A:LYS178 4.5 15.3 1.0
C A:LEU180 4.6 8.0 1.0
O A:ARG176 4.6 11.7 1.0
O6A A:MYA504 4.7 7.9 1.0
CG A:LEU180 4.8 10.0 1.0
CG2 A:VAL171 4.8 7.5 1.0
CB A:VAL171 4.9 7.1 1.0

Reference:

J.A.Brannigan, J.A.Brannigan. N/A N/A.
Page generated: Tue Oct 1 15:27:30 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy