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: Mon Dec 14 23:52:16 2020

Last articles

Zn in 7VD8
Zn in 7V1R
Zn in 7V1Q
Zn in 7VPF
Zn in 7T85
Zn in 7T5F
Zn in 7NF9
Zn in 7M4M
Zn in 7M4O
Zn in 7M4N
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy