One lineage, side by side
Every structure here was aligned onto IsPETase 6EQE when it was written, so these panels are already in register: rotating one rotates all of them, and the same view means the same orientation in every panel. The catalytic triad is drawn in yellow and substituted residues in pink, using the residues the geometry stage measured rather than positions inferred from an alignment.
The question this asks, which the catalogue cannot: do stabilising mutations keep clear of the catalytic machinery, or do some crowd it? Every substituted residue carries its side-chain distance to the nearest triad side chain, measured once from these coordinates. The wild types group asks a different question with the same machinery: those are natural enzymes from unrelated organisms that nobody has engineered, so what varies between them is what evolution did rather than what a protein engineer did.
Cut190 lineage
Cut190 wild type
crystal structure 4WFI, 1.45 Å · cleft 16.6 Å
Cut190**SS
crystal structure 7CTR, 1.2 Å · 7 substitutions · cleft 16.4 Å
nearest substitution to the triad: 4.9 Å (PRO)
Distances are side chain to side chain, excluding backbone atoms. Measured any-atom to any-atom they came out at 1.31–1.35 Å for four variants, which is a peptide bond rather than a contact: those residues simply sit next to a triad residue in sequence. Where a substituted residue is adjacent in sequence it is marked, so a short distance that only reflects the fold's connectivity is visible as such.
Sequences one per panel above, in the same order
catalytic triad substitution against the lineage wild type · triad positions are labelled; hover any residue for its number. Click one to select it in its panel above, or click a residue in a panel to find it here.