Figure 3.
Fig. 3. Structure of apoCmaA1. a, superimposition of C[
]atoms
of structures of apoCmaA1 (gray) and CmaAl-SAH-DDDMAB (blue)
using residues 20-170. Residues 136-145 and residues 170-210 of
apoCmaA1 are colored in green. b, comparison of the active site
cavities in apoCmaA1 and CmaAl-SAH-DDDMAB.
The above figure is reprinted
by permission from the ASBMB:
J Biol Chem
(2002,
277,
11559-11569)
copyright 2002.
]atoms
of structures of apoCmaA1 (gray) and CmaAl-SAH-DDDMAB (blue)
using residues 20-170. Residues 136-145 and residues 170-210 of
apoCmaA1 are colored in green. b, comparison of the active site
cavities in apoCmaA1 and CmaAl-SAH-DDDMAB.