Research workbench
AlphaFold monomer V2.0 prediction for variant surface glycoprotein iltat 1.22 (P26327)
Analyse AlphaFold monomer V2.0 prediction for variant surface glycoprotein iltat 1.22… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P26327
- Type
- protein
- Length
- 479 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd1A2963012bEcbC7A8f505464439Ab678C48936f
- Molecule
- Variant surface glycoprotein iltat 1.22
- UniProt
- P26327
- Pockets
- 4 · best druggability 0.54
Structure
1 distinct chain · 42% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Variant surface glycoprotein iltat 1.22 | protein | 479 | 42% helix, 13% strand | P26327 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 210 | 0.54 | 0.78 | 33 | empty |
| 2 | 52 | 0.31 | 0.77 | 16 | empty |
| 3 | 52 | 0.28 | 0.75 | 13 | empty |
| 4 | 57 | 0.27 | 0.74 | 17 | 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 P26327
- Elsewhere: UniProt P26327 · AlphaFold DB P26327
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