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.
Structures with no assigned lineage · 37–48 of 534
ACS:52fc95dcc8
ESMFold prediction, pLDDT 94 · cleft 17.1 Å
ACS:5395363d08
ESMFold prediction, pLDDT 94 · cleft 20.4 Å
ACS:53bb91a909
ESMFold prediction, pLDDT 90 · cleft 21.0 Å
ACS:57ae927ff6
ESMFold prediction, pLDDT 89 · cleft 23.6 Å
ACS:5a664c7a2a
ESMFold prediction, pLDDT 92 · cleft 18.3 Å
ACS:5b23f37b97
ESMFold prediction, pLDDT 92 · cleft 17.0 Å
ACS:5d687d13c2
ESMFold prediction, pLDDT 92 · cleft 17.1 Å
ACS:5e57c5543b
ESMFold prediction, pLDDT 45
no triad measurable — this deposit is a catalytically inactivated form, with the nucleophilic serine replaced by alanine so the enzyme could be crystallised with substrate bound. The fold and every engineered substitution are right; the catalytic residue is simply not in the model, so the panel shows the whole molecule.
ACS:5ffe0c10cc
ESMFold prediction, pLDDT 91 · cleft 19.7 Å
ACS:62c5c39a5e
ESMFold prediction, pLDDT 89 · cleft 22.9 Å
ACS:662cf89264
ESMFold prediction, pLDDT 88 · cleft 26.2 Å
ACS:67ad0990a4
ESMFold prediction, pLDDT 95 · cleft 17.0 Å
ACS:5e57c5543b has no measurable triad, and the reason is the deposit rather than the enzyme: these are inactivated crystallisation constructs with the catalytic serine mutated to alanine. Everything else about them is correct, including every engineered substitution, and the sequence held here is the active enzyme — only the coordinates are the knockout.
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. Panels built from predictions carry the loops that gate the cleft at lower confidence than the crystal structures beside them; a distance measured on one is weaker evidence than the same distance measured on the other.
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.