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PETase ANnotation and Triage System

Nature's solution to a human-made health problem

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 · 1–12 of 534

ACS:047e314722

ESMFold prediction, pLDDT 89 · cleft 25.7 Å

ACS:060a8d6878

ESMFold prediction, pLDDT 91 · cleft 17.1 Å

ACS:08a2e84bd3

ESMFold prediction, pLDDT 90 · cleft 24.0 Å

ACS:0a514d39db

ESMFold prediction, pLDDT 89 · cleft 24.2 Å

ACS:0b55a34f83

ESMFold prediction, pLDDT 93 · cleft 15.1 Å

ACS:12ebcfd3a8

ESMFold prediction, pLDDT 93 · cleft 23.4 Å

ACS:19ae3c0284

ESMFold prediction, pLDDT 90 · cleft 20.5 Å

ACS:1a7b1489c5

ESMFold prediction, pLDDT 96 · cleft 22.0 Å

ACS:1a8d234c1f

ESMFold prediction, pLDDT 87 · cleft 23.5 Å

ACS:1b66fe9bab

ESMFold prediction, pLDDT 95 · cleft 22.2 Å

ACS:1bdd778aad

ESMFold prediction, pLDDT 93 · cleft 21.1 Å

ACS:1e7e8c945d

ESMFold prediction, pLDDT 89 · cleft 23.9 Å

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.