Figure 4.
Fig. 4 View of the P-3-H active site. The active site of
the enzyme (molecule A) cocrystallized with iron(II) sulfate.
The -barrel core
is in green, the iron binding ligands in purple, the iron in
orange and the N-terminal region and C-terminal domain in
magenta. The ferrous iron is ligated by the side chains of
His107, Asp109 and His158. Note: (a) Arg168, Ser170 and His135
which are probably involved in binding 2-OG; (b) Arg95, Arg97,
Arg122 and His43 which may bind the proline carboxylate; (c) the
disordered loop (in orange) containing six sequential acidic
residues, which may bind the imino group of proline.
The above figure is reprinted
by permission from the Federation of European Biochemical Societies:
Eur J Biochem
(2001,
268,
6625-6636)
copyright 2001.
-barrel core
is in green, the iron binding ligands in purple, the iron in
orange and the N-terminal region and C-terminal domain in
magenta. The ferrous iron is ligated by the side chains of
His107, Asp109 and His158. Note: (a) Arg168, Ser170 and His135
which are probably involved in binding 2-OG; (b) Arg95, Arg97,
Arg122 and His43 which may bind the proline carboxylate; (c) the
disordered loop (in orange) containing six sequential acidic
residues, which may bind the imino group of proline.