FAST-PETase-N212A/K233C/S282C
290 aa · engineered from IsPETase · Li et al. 2025, Int. J. Biol. Macromol.
Structure, superposed on IsPETase
Aligned onto IsPETase 6EQE when it was written, so anything added below overlays directly and the browser does no alignment. The catalytic triad is drawn from the residues the geometry stage measured, not from positions inferred by an alignment.
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Sequence 290 aa · 7 substitutions
catalytic triad substitution against IsPETase · the same colours as the viewer above. Triad positions are labelled; hover any residue for its number. Click one to select it in both.
Activity
| Optimum temperature | not recorded |
| Optimum pH | not recorded |
| Family | petase_like |
Structure
| Source | Experimental, PDB 9LMS |
| Resolution | 1.71 Å |
| Residues | 262 |
| Cα RMSD to IsPETase | 0.26 Å |
Active site
| Catalytic triad | Ser160 · His237 · Asp206 |
| Ser OG → His NE2 | 2.65 Å |
| His ND1 → Asp OD | 3.14 Å |
| Oxyanion donor 1 | 161 (3.09 Å) |
| Oxyanion donor 2 | 87 (4.91 Å) |
| Cleft width | 21.93 Å |
| Cleft depth | 4.34 Å |
| Cleft residues | 84 |
Aromatic clamp: PHE201 · TRP159 · TRP185 · TYR219 · TYR87
Mutations
S121E, D186H, N212A, R224Q, N233C, R280A, S282C
7 substitutions against IsPETase. Every one was applied by a routine that refuses any substitution whose stated parent residue does not match, so a wrong position or a mature-versus-precursor numbering shift fails loudly rather than producing a plausible but wrong sequence.
A disulfide-stabilised FAST-PETase, from PDB 9LMS at 1.71 A. Expressed against IsPETase rather than against FAST-PETase, because IsPETase is the root of this lineage and every other member is quoted the same way: it is FAST-PETase's five with N233K taken on to N233C, plus N212A and S282C. C233 and C282 form an engineered disulfide across the SAME residue pair Z1-PETase uses, reached independently by a different group. Verified by aligning 9LMS's mature chain to FAST-PETase, which differs at exactly the three positions its deposit title names.
Reference: Li et al. 2025, Int. J. Biol. Macromol. doi:10.1016/j.ijbiomac.2025.145862
Measured activity
No measurement rows. The enzyme is in the reference set on the strength of its curation source rather than a value extracted into this database.
Related in PANTS
Lineage
Engineered from IsPETase.
Nearest metagenomic candidates
No candidate in the catalogue names this enzyme as its nearest match.
Identifiers and cross-references
A disulfide-stabilised FAST-PETase, from PDB 9LMS at 1.71 A. Expressed against IsPETase rather than against FAST-PETase, because IsPETase is the root of this lineage and every other member is quoted the same way: it is FAST-PETase's five with N233K taken on to N233C, plus N212A and S282C. C233 and C282 form an engineered disulfide across the SAME residue pair Z1-PETase uses, reached independently by a different group. Verified by aligning 9LMS's mature chain to FAST-PETase, which differs at exactly the three positions its deposit title names.