One protein, before and after it is switched on by being
cut. Superposed on shared residue numbering, so switching shows the
chain come apart and nothing else move. Bovine.
structure
site
colour
what you are looking at
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chains drawn
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spans
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modelled
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completeness
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disulfides
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in the site
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helix / strand
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extents Å
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superposed on
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ligands
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view
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The numbering is shared. Both entries number in
chymotrypsinogen numbering, so the superposition is a match on
residue number rather than a sequence alignment, and residue 57 is
His57 in both files.
Two cuts, not one. Trypsin cuts 15–16 and
makes the enzyme; chymotrypsin then excises the dipeptides
14–15 and 147–148 from its own kind. Three chains is the
result of the second.
Nothing is bound in either file. Water only, so
the site is drawn empty in both — which is what lets the two
pockets be compared at all.
Turn the molecule, then copy. Both
structures share one rotation basis, so one choice re-aims them together.
Paste it into view.basis in proteins.js with
by: 'human'.