Figure 4.
Figure 4. Stereo images with details of the novel
ligand-binding site in FluA. (A) 2F[o]-F[c] electron density for
the bound fluorescein contoured at 1.0 ,
together with sidechains of residues closer than 3.8 Å.
Amino acids that were mutated in FluA (cf. Fig. 1) are colored
dark-green, whereas original residues of BBP are depicted in
light-green. (B) The set of 16 randomly mutated sidechains in
the FluA crystal structure with the complexed fluorescein. (C)
Arrangement of positively charged residues at the entrance to
the ligand pocket of FluA. The three characteristically arranged
Arg side chains (see text) are colored dark-blue. Note that
there is a considerable distance between Arg 95 - whose
sidechain is well defined in the electron density - and the
bound fluorescein along the view axis (distance between the
guanidinium and carboxylate groups: 8.6 Å) such that no
direct contact is formed.
The above figure is reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2003,
53,
121-129)
copyright 2003.
,
together with sidechains of residues closer than 3.8 Å.
Amino acids that were mutated in FluA (cf. Fig. 1) are colored
dark-green, whereas original residues of BBP are depicted in
light-green. (B) The set of 16 randomly mutated sidechains in
the FluA crystal structure with the complexed fluorescein. (C)
Arrangement of positively charged residues at the entrance to
the ligand pocket of FluA. The three characteristically arranged
Arg side chains (see text) are colored dark-blue. Note that
there is a considerable distance between Arg 95 - whose
sidechain is well defined in the electron density - and the
bound fluorescein along the view axis (distance between the
guanidinium and carboxylate groups: 8.6 Å) such that no
direct contact is formed.