LCC-A2
293 aa · engineered from LCC · Orr et al. 2024, Biotechnol. J.
LCC-ICCG plus H218Y/N248D; >90% depolymerisation at 200 g/kg in 3.3 h
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 293 aa · 6 substitutions
catalytic triad substitution against LCC · 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 | 78.0 °C |
| As published | Published as 78 °C. |
| Optimum pH | not recorded |
| Family | cutinase |
Structure
| Source | ESMFold prediction |
| Mean pLDDT | 96.0 |
| Residues | 293 |
| Cα RMSD to IsPETase | 1.63 Å |
Active site
| Catalytic triad | Ser165 · His242 · Asp210 |
| Ser OG → His NE2 | 2.93 Å |
| His ND1 → Asp OD | 2.93 Å |
| Oxyanion donor 1 | 166 (2.87 Å) |
| Oxyanion donor 2 | 95 (4.51 Å) |
| Cleft width | 18.84 Å |
| Cleft depth | 4.36 Å |
| Cleft residues | 82 |
Aromatic clamp: PHE125 · PHE222 · TRP190 · TYR218 · TYR95
Mutations
F243I, D238C, S283C, Y127G, H218Y, N248D
6 substitutions against LCC. 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.
LCC-ICCG plus H218Y/N248D, Topt 78 C. Built ON LCC-ICCG, not on wild-type LCC: its six substitutions are ICCG's four plus H218Y and N248D, verified as a strict superset. The display nests it under ICCG accordingly. Expressed here against WILD-TYPE LCC (all six mutations, offset 0) rather than against LCC-ICCG, because a variant can only be derived from a parent in WILD_TYPES and chaining a variant onto a variant would hide which residues were actually checked.
Reference: Orr et al. 2024, Biotechnol. J. doi:10.1002/biot.202400021
Measured activity
| Parameter | Value | Substrate | Evidence | Source |
|---|---|---|---|---|
| performance claim | — | PET | from review | 10.1002/biot.202400021 |
| LCC-ICCG plus H218Y/N248D; >90% depolymerisation at 200 g/kg in 3.3 h | ||||
| topt | 78.0 degC | PET | from review | 10.1002/biot.202400021 |
| Published as 78 °C. | ||||
Related in PANTS
Lineage
Engineered from LCC.
Nearest metagenomic candidates
No candidate in the catalogue names this enzyme as its nearest match.
Identifiers and cross-references
Activity
Internal
LCC-ICCG plus H218Y/N248D, Topt 78 C. Built ON LCC-ICCG, not on wild-type LCC: its six substitutions are ICCG's four plus H218Y and N248D, verified as a strict superset. The display nests it under ICCG accordingly. Expressed here against WILD-TYPE LCC (all six mutations, offset 0) rather than against LCC-ICCG, because a variant can only be derived from a parent in WILD_TYPES and chaining a variant onto a variant would hide which residues were actually checked.