Figure 1.
Figure 1. Structure of D1 protease. a, Ribbon drawing of D1P.
The A domain is in red, the B domain in yellow and the C domain
in blue. The extended -hairpin
loop from the C domain forms an integral part of the folding
domain A and is regarded as part of that domain. The loops that
connect domains A to B and B to C have very high temperature
factors and are colored in green. The side chains of the
residues involved in catalysis or substrate binding, K397, S372
and R247, are shown in ball-and-stick representation. The GVGL
loop in the B domain, highlighted in magenta, has been shown to
be involved in the binding of the C-terminal residues of the
peptide ligand in the structurally homologous third PDZ domain
of synaptic protein PSD-95^25. b, Stereo view of the C trace
of D1P. Every 10^th residue and the N-terminus and C-terminus
are labeled. The disulfide bond between Cys 260 and Cys 451 is
shown in yellow. The orientation of the molecule is the same as
the standard orientation in (a).
-hairpin
loop from the C domain forms an integral part of the folding
domain A and is regarded as part of that domain. The loops that
connect domains A to B and B to C have very high temperature
factors and are colored in green. The side chains of the
residues involved in catalysis or substrate binding, K397, S372
and R247, are shown in ball-and-stick representation. The GVGL
loop in the B domain, highlighted in magenta, has been shown to
be involved in the binding of the C-terminal residues of the
peptide ligand in the structurally homologous third PDZ domain
of synaptic protein PSD-95^25. b, Stereo view of the C 
trace
of D1P. Every 10^th residue and the N-terminus and C-terminus
are labeled. The disulfide bond between Cys 260 and Cys 451 is
shown in yellow. The orientation of the molecule is the same as
the standard orientation in (a).