Research workbench
AlphaFold monomer V2.0 prediction for POLY(3-hydroxyalkanoate) depolymerase (P26495)
Analyse AlphaFold monomer V2.0 prediction for POLY(3-hydroxyalkanoate) depolymerase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P26495
- Type
- protein
- Length
- 283 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x41C049aD5427907F76fA6Cdd2DB97E59526d6E41
- Molecule
- POLY(3-hydroxyalkanoate) depolymerase
- UniProt
- P26495
- Pockets
- 2 · best druggability 0.72
Structure
1 distinct chain · 41% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | POLY(3-hydroxyalkanoate) depolymerase | protein | 283 | 41% helix, 18% strand | P26495 |
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 72 | 0.72 | 0.97 | 22 | empty |
| 2 | 261 | 0.67 | 0.83 | 24 | empty |
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P26495
- Elsewhere: UniProt P26495 · AlphaFold DB P26495
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