Atomistry » Magnesium » PDB 6q70-6qiu » 6qdc
Atomistry »
  Magnesium »
    PDB 6q70-6qiu »
      6qdc »

Magnesium in PDB 6qdc: Leishmania Major N-Myristoyltransferase in Complex with Thienopyrimidine Inhibitor Imp-0000101

Enzymatic activity of Leishmania Major N-Myristoyltransferase in Complex with Thienopyrimidine Inhibitor Imp-0000101

All present enzymatic activity of Leishmania Major N-Myristoyltransferase in Complex with Thienopyrimidine Inhibitor Imp-0000101:
2.3.1.97;

Protein crystallography data

The structure of Leishmania Major N-Myristoyltransferase in Complex with Thienopyrimidine Inhibitor Imp-0000101, PDB code: 6qdc 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 / 1.40
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 47.672, 90.638, 53.113, 90.00, 111.75, 90.00
R / Rfree (%) 17.1 / 20.8

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Leishmania Major N-Myristoyltransferase in Complex with Thienopyrimidine Inhibitor Imp-0000101 (pdb code 6qdc). 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-0000101, PDB code: 6qdc:

Magnesium binding site 1 out of 1 in 6qdc

Go back to Magnesium Binding Sites List in 6qdc
Magnesium binding site 1 out of 1 in the Leishmania Major N-Myristoyltransferase in Complex with Thienopyrimidine Inhibitor Imp-0000101


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-0000101 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1002

b:20.7
occ:1.00
O A:LEU175 2.8 16.5 1.0
O1A A:MYA1001 2.8 11.9 1.0
N A:LYS178 2.9 15.4 1.0
O5A A:MYA1001 3.0 13.4 1.0
N A:LEU180 3.1 12.5 1.0
N A:ARG179 3.4 14.0 1.0
N A:GLU177 3.4 14.2 1.0
CB A:LEU180 3.4 14.5 1.0
CA A:LYS178 3.5 17.2 1.0
C A:LYS178 3.6 16.4 1.0
P1A A:MYA1001 3.6 12.3 1.0
CB A:LYS178 3.7 19.2 1.0
O2A A:MYA1001 3.7 13.4 1.0
C A:ARG176 3.7 16.1 1.0
CA A:LEU180 3.8 13.3 1.0
C A:LEU175 3.9 14.6 1.0
CA A:ARG176 4.0 15.0 1.0
C A:GLU177 4.0 17.1 1.0
CG1 A:VAL171 4.1 12.6 1.0
C A:ARG179 4.1 15.5 1.0
P2A A:MYA1001 4.1 12.3 1.0
CA A:GLU177 4.2 16.6 1.0
CA A:ARG179 4.2 14.3 1.0
N A:ALA181 4.3 12.2 1.0
O3A A:MYA1001 4.3 12.1 1.0
O A:LYS178 4.4 19.2 1.0
N A:ARG176 4.4 14.9 1.0
O A:ARG176 4.5 17.9 1.0
C A:LEU180 4.6 12.6 1.0
CG A:LYS178 4.6 21.9 1.0
O6A A:MYA1001 4.7 11.5 1.0
CG2 A:VAL171 4.7 11.3 1.0
CG A:LEU180 4.8 17.2 1.0
CB A:VAL171 4.9 10.1 1.0
CD2 A:LEU180 5.0 17.5 1.0

Reference:

J.A.Brannigan, J.A.Brannigan. N/A N/A.
Page generated: Tue Oct 1 15:27:23 2024

Last articles

Zn in 9J0N
Zn in 9J0O
Zn in 9J0P
Zn in 9FJX
Zn in 9EKB
Zn in 9C0F
Zn in 9CAH
Zn in 9CH0
Zn in 9CH3
Zn in 9CH1
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy