Research workbench
AlphaFold monomer V2.0 prediction for post-gpi attachment to proteins factor 3 (Q96FM1)
Analyse AlphaFold monomer V2.0 prediction for post-gpi attachment to proteins factor 3… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q96FM1
- Type
- protein
- Length
- 320 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x854ac6A396D6e8Ea3EFbfaDbB10Bb9DBe804468b
- Molecule
- Post-gpi attachment to proteins factor 3
- UniProt
- Q96FM1
- Pockets
- 2 · best druggability 0.84
Structure
1 distinct chain · 77% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Post-gpi attachment to proteins factor 3 | protein | 320 | 77% helix, 2% strand | Q96FM1 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1031 | 0.84 | 0.85 | 75 | empty |
| 2 | 53 | 0.26 | 0.73 | 16 | empty |
Modifications
Observed in the structure: 3 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 Q96FM1
- Elsewhere: UniProt Q96FM1 · AlphaFold DB Q96FM1
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