Figure 3.
(a) Overall structure of VcMTAN showing the asymmetric unit
content with the inhibitor BuT-DADMe-ImmA bound in the active
sites. (b) The active site of VcMTAN with a 2F[o] - F[c] map
contoured at 1.2 surrounding
the BuT-DADMe-ImmA inhibitor and the proposed nucleophilic water
molecule. (c) Space-filling picture of the active site of VcMTAN
with BuT-DADMe-ImmA in the active site. Grey represents
hydrophobic regions of the protein, which interact with
hydrophobic parts of the inhibitor. The red color shows parts of
the protein that contain charged residues interacting with polar
groups of the inhibitor, and green represents loop regions. (d)
Schematic drawing of the BuT-DADMe-ImmA inhibitor bound in the
active site of VcMTAN showing catalytic contacts.
The above figure is reprinted
from an Open Access publication published by Macmillan Publishers Ltd:
Nat Chem Biol
(2009,
5,
251-257)
copyright 2009.
surrounding
the BuT-DADMe-ImmA inhibitor and the proposed nucleophilic water
molecule. (c) Space-filling picture of the active site of VcMTAN
with BuT-DADMe-ImmA in the active site. Grey represents
hydrophobic regions of the protein, which interact with
hydrophobic parts of the inhibitor. The red color shows parts of
the protein that contain charged residues interacting with polar
groups of the inhibitor, and green represents loop regions. (d)
Schematic drawing of the BuT-DADMe-ImmA inhibitor bound in the
active site of VcMTAN showing catalytic contacts.