Cut190
Saccharomonospora viridis · 304 aa · UniProt
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
catalytic triad · 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 | cutinase |
Structure
| Source | Experimental, PDB 4WFI |
| Resolution | 1.45 Å |
| Residues | 258 |
| Cα RMSD to IsPETase | 1.89 Å |
Active site
| Catalytic triad | Ser176 · His254 · Asp222 |
| Ser OG → His NE2 | 2.70 Å |
| His ND1 → Asp OD | 3.12 Å |
| Oxyanion donor 1 | 177 (3.10 Å) |
| Cleft width | 16.60 Å |
| Cleft depth | 4.05 Å |
| Cleft residues | 82 |
Aromatic clamp: PHE106 · PHE234 · PHE255 · TRP201
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
Variants built on this enzyme:
Cut190**SS
Nearest metagenomic candidates
1 candidate in the catalogue have this as their nearest characterised enzyme.
Identifiers and cross-references
Sequence
Saccharomonospora viridis AHK190 cutinase, 304 aa. STRAIN AMBIGUITY RESOLVED 2026-08-05: UniProt carries two 304 aa entries for this organism, W0TJ64 and C7MVE8 (type strain P101), and length alone cannot separate them. The Cut190 crystal structures settle it: 4WFI, 4WFJ, 4WFK, 5ZNO, 5ZRQ and 5ZRR all cross-reference W0TJ64, and C7MVE8 has no PDB entry at all. Structural evidence over a name match.