Figure 2.
Figure 2. (A) Ribbon diagram of the Anabaena sp. AGT dimer. The
N-terminal segment (red), N-terminal domain (green), and
C-terminal domain (blue) are indicated for chain A. (B)
Superposition of Anabaena sp. AGT (blue) and human AGT (PDB
code: 1h0c; gray). The corresponding bound PLP and LLP
(lysine-pyridoxal-5 -phosphate)
ligands are shown in ball-and-stick representation, and regions
of structural difference are labeled. (C) The PLP molecule bound
to the active site of Anabaena sp. AGT and interacting residues
are shown in ball-and-stick representation. 2Fo-Fc density for
PLP contoured at 1 is
shown in blue. (D) Superposition of the active sites with the
PLP and LLP molecules and interacting residues from Anabaena sp.
AGT (blue) and their counterparts in human AGT (gray, residues
labeled in brackets) in ball-and-stick representation.
The above figure is reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2005,
58,
971-975)
copyright 2005.
-phosphate)
ligands are shown in ball-and-stick representation, and regions
of structural difference are labeled. (C) The PLP molecule bound
to the active site of Anabaena sp. AGT and interacting residues
are shown in ball-and-stick representation. 2Fo-Fc density for
PLP contoured at 1 
is
shown in blue. (D) Superposition of the active sites with the
PLP and LLP molecules and interacting residues from Anabaena sp.
AGT (blue) and their counterparts in human AGT (gray, residues
labeled in brackets) in ball-and-stick representation.