IsPETase-W159H/S238F
290 aa · engineered from IsPETase · Austin et al. 2018, PNAS
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.
Overlay another
Sequence 290 aa · 2 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 6EQF |
| Resolution | 1.7 Å |
| Residues | 269 |
| Cα RMSD to IsPETase | 1.27 Å |
Active site
| Catalytic triad | Ser160 · His237 · Asp206 |
| Ser OG → His NE2 | 2.89 Å |
| His ND1 → Asp OD | 3.02 Å |
| Oxyanion donor 1 | 161 (3.28 Å) |
| Oxyanion donor 2 | 87 (5.55 Å) |
| Cleft width | 22.09 Å |
| Cleft depth | 4.21 Å |
| Cleft residues | 82 |
Aromatic clamp: PHE201 · TRP159 · TRP185 · TYR219 · TYR87
Mutations
W159H, S238F
2 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.
The narrowed-cleft double mutant: the experiment that showed the PETase cleft is wider than a cutinase's and that narrowing it changes activity.
Reference: Austin et al. 2018, PNAS doi:10.1073/pnas.1718804115
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
The narrowed-cleft double mutant: the experiment that showed the PETase cleft is wider than a cutinase's and that narrowing it changes activity.