########     ###    ##    ## ########  ######  
##     ##   ## ##   ###   ##    ##    ##    ## 
##     ##  ##   ##  ####  ##    ##    ##       
########  ##     ## ## ## ##    ##     ######  
##        ######### ##  ####    ##          ## 
##        ##     ## ##   ###    ##    ##    ## 
##        ##     ## ##    ##    ##     ######  

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 · 157–168 of 534

PAZy:175

ESMFold prediction, pLDDT 94 · cleft 18.6 Å

PAZy:176

ESMFold prediction, pLDDT 94 · cleft 18.6 Å

PAZy:177

AlphaFold model · cleft 18.8 Å

PAZy:178

crystal structure 8AIR, 1.08 Å · cleft 22.5 Å

PAZy:179

crystal structure 8AIS, 1.56 Å · cleft 19.7 Å

PAZy:18

crystal structure 7CEF, 1.6 Å · cleft 20.0 Å

PAZy:180

crystal structure 8AIT, 1.24 Å · cleft 23.7 Å

PAZy:181

crystal structure 8C65, 1.49 Å · cleft 20.3 Å

PAZy:182

crystal structure 5AJH, 1.9 Å · cleft 14.3 Å

PAZy:183

AlphaFold model · cleft 20.2 Å

PAZy:184

AlphaFold model · cleft 22.8 Å

PAZy:185

crystal structure 9HYD, 1.43 Å · cleft 19.8 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.