Research workbench
AlphaFold monomer V2.0 prediction for ribulose bisphosphate carboxylase large chain (A2C106)
Analyse AlphaFold monomer V2.0 prediction for ribulose bisphosphate carboxylase large… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A2C106
- Type
- protein
- Length
- 470 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbff27Dc0a932A6E0d9Fe883AAbD1BF27bB95A69F
- Molecule
- Ribulose bisphosphate carboxylase large chain
- UniProt
- A2C106
- Pockets
- 5 · best druggability 0.61
Structure
1 distinct chain · 42% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribulose bisphosphate carboxylase large chain | protein | 470 | 42% helix, 18% strand | A2C106 |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 77 | 0.61 | 0.90 | 16 | empty |
| 2 | 169 | 0.51 | 0.78 | 28 | empty |
| 3 | 143 | 0.51 | 0.79 | 24 | empty |
| 4 | 82 | 0.33 | 0.74 | 16 | empty |
| 5 | 62 | 0.32 | 0.75 | 14 | empty |
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 A2C106
- Elsewhere: UniProt A2C106 · AlphaFold DB A2C106
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