Research workbench
AlphaFold monomer V2.0 prediction for non-functional protein stay- green, chloroplastic (A7VLV2)
Analyse AlphaFold monomer V2.0 prediction for non-functional protein stay- green… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A7VLV2
- Type
- protein
- Length
- 263 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4d07E6a23DeB6B95bd9b90EcB67368b7e8D3B77e
- Molecule
- Non-functional protein stay-green, chloroplastic
- UniProt
- A7VLV2
- Pockets
- 4 · best druggability 0.74
Structure
1 distinct chain · 24% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Non-functional protein stay-green, chloroplastic | protein | 263 | 24% helix, 21% strand | A7VLV2 |
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 | 370 | 0.74 | 0.85 | 33 | empty |
| 2 | 397 | 0.63 | 0.78 | 43 | empty |
| 3 | 72 | 0.32 | 0.75 | 14 | empty |
| 4 | 55 | 0.31 | 0.76 | 21 | empty |
Modifications
Observed in the structure: 1 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 A7VLV2
- Elsewhere: UniProt A7VLV2 · AlphaFold DB A7VLV2
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