Research workbench
AlphaFold monomer V2.0 prediction for pectin acetylesterase 9 (B9DFR3)
Analyse AlphaFold monomer V2.0 prediction for pectin acetylesterase 9 (B9DFR3) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B9DFR3
- Type
- protein
- Length
- 451 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbb2F1C7CB3A1eeFAc24fCa72cc627162D5413FD7
- Molecule
- Pectin acetylesterase 9
- UniProt
- B9DFR3
- Pockets
- 4 · best druggability 0.61
Structure
1 distinct chain · 39% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pectin acetylesterase 9 | protein | 451 | 39% helix, 14% strand | B9DFR3 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 162 | 0.61 | 0.84 | 32 | empty |
| 2 | 200 | 0.52 | 0.77 | 29 | empty |
| 3 | 79 | 0.36 | 0.77 | 19 | empty |
| 4 | 57 | 0.36 | 0.79 | 15 | empty |
Modifications
Observed in the structure: 8 disulfide (disulfide).
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 B9DFR3
- Elsewhere: UniProt B9DFR3 · AlphaFold DB B9DFR3
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