Research workbench
AlphaFold monomer V2.0 prediction for gdsl ESTERASE/LIPASE AT1G28570 (Q9FXJ1)
Analyse AlphaFold monomer V2.0 prediction for gdsl ESTERASE/LIPASE AT1G28570 (Q9FXJ1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9FXJ1
- Type
- protein
- Length
- 389 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x738c1929c69B751bD0Be0B962D9bac20B631aAc6
- Molecule
- Gdsl ESTERASE/LIPASE AT1G28570
- UniProt
- Q9FXJ1
- Pockets
- 2 · best druggability 0.77
Structure
1 distinct chain · 43% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Gdsl ESTERASE/LIPASE AT1G28570 | protein | 389 | 43% helix, 9% strand | Q9FXJ1 |
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 | 104 | 0.77 | 0.97 | 27 | empty |
| 2 | 401 | 0.72 | 0.83 | 36 | empty |
Modifications
Observed in the structure: 5 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 Q9FXJ1
- Elsewhere: UniProt Q9FXJ1 · AlphaFold DB Q9FXJ1
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