Research workbench
AlphaFold monomer V2.0 prediction for ribulose bisphosphate carboxylase large chain (P26490)
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
- P26490
- Type
- protein
- Length
- 475 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xBF0D2e107Ce1EcD2C4369B042274201DB719AaAF
- Molecule
- Ribulose bisphosphate carboxylase large chain
- UniProt
- P26490
- Pockets
- 4 · best druggability 0.68
Structure
1 distinct chain · 43% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribulose bisphosphate carboxylase large chain | protein | 475 | 43% helix, 16% strand | P26490 |
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 | 87 | 0.68 | 0.93 | 22 | empty |
| 2 | 161 | 0.49 | 0.77 | 29 | empty |
| 3 | 143 | 0.47 | 0.78 | 25 | empty |
| 4 | 67 | 0.30 | 0.73 | 16 | 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 P26490
- Elsewhere: UniProt P26490 · AlphaFold DB P26490
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