Cut190**SS
304 aa · engineered from Cut190 · Oda et al. 2018, Appl. Microbiol. Biotechnol.
Disulfide-stabilised; calcium-dependent conformational switching
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 304 aa · 7 substitutions
catalytic triad substitution against Cut190 · 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 | 65.0 °C |
| As published | Published as 65 °C. |
| Optimum pH | not recorded |
| Family | cutinase |
Structure
| Source | Experimental, PDB 7CTR |
| Resolution | 1.2 Å |
| Residues | 259 |
| Cα RMSD to IsPETase | 1.90 Å |
Active site
| Catalytic triad | Ser176 · His254 · Asp222 |
| Ser OG → His NE2 | 2.73 Å |
| His ND1 → Asp OD | 3.22 Å |
| Oxyanion donor 1 | 177 (3.03 Å) |
| Cleft width | 16.36 Å |
| Cleft depth | 4.15 Å |
| Cleft residues | 83 |
Aromatic clamp: PHE106 · PHE234 · PHE255 · TRP201
Mutations
Q123H, Q138A, N202H, S226P, R228S, D250C, E296C
7 substitutions against Cut190. 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.
Disulfide-stabilised Cut190. CORRECTED after a literature check: this entry previously took its sequence from PDB 7CEF, which is Cut190* (S226P/R228S with a C-terminal truncation) and carries only the two native cysteines. The 'SS' in the name IS an engineered disulfide, so an entry without one was the wrong molecule under the right name. 7CTR is the real variant: 4 cysteines, and D250C/E296C form the added bridge. All seven published substitutions match Cut190 at offset 0 and take the cysteine count from 2 to 4, which is the check that settles it.
Reference: Oda et al. 2018, Appl. Microbiol. Biotechnol. doi:10.1007/s00253-018-9374-x
Measured activity
| Parameter | Value | Substrate | Evidence | Source |
|---|---|---|---|---|
| performance claim | — | PET | from review | 10.1007/s00253-018-9374-x |
| Disulfide-stabilised; calcium-dependent conformational switching | ||||
| topt | 65.0 degC | PET | from review | 10.1007/s00253-018-9374-x |
| Published as 65 °C. | ||||
Related in PANTS
Lineage
Engineered from Cut190.
Nearest metagenomic candidates
No candidate in the catalogue names this enzyme as its nearest match.
Identifiers and cross-references
Disulfide-stabilised Cut190. CORRECTED after a literature check: this entry previously took its sequence from PDB 7CEF, which is Cut190* (S226P/R228S with a C-terminal truncation) and carries only the two native cysteines. The 'SS' in the name IS an engineered disulfide, so an entry without one was the wrong molecule under the right name. 7CTR is the real variant: 4 cysteines, and D250C/E296C form the added bridge. All seven published substitutions match Cut190 at offset 0 and take the cysteine count from 2 to 4, which is the check that settles it.