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AlphaFold monomer V2.0 prediction for post-gpi attachment to proteins factor 3 (A2V7M9)
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
- A2V7M9
- Type
- protein
- Length
- 320 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xb6B6a8B1b9C758652293B6ae405d26F422203cef
- Molecule
- Post-gpi attachment to proteins factor 3
- UniProt
- A2V7M9
- 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 | A2V7M9 |
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 | 752 | 0.84 | 0.87 | 70 | empty |
| 2 | 51 | 0.33 | 0.77 | 9 | 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 A2V7M9
- Elsewhere: UniProt A2V7M9 · AlphaFold DB A2V7M9
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