Research workbench
AlphaFold monomer V2.0 prediction for ribulose bisphosphate carboxylase large chain (P25414)
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
- P25414
- Type
- protein
- Length
- 421 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xBb37fE2B3777b9cf6A94E8e4EF413FcB6B83A32E
- Molecule
- Ribulose bisphosphate carboxylase large chain
- UniProt
- P25414
- Pockets
- 5 · best druggability 0.75
Structure
1 distinct chain · 46% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribulose bisphosphate carboxylase large chain | protein | 421 | 46% helix, 14% strand | P25414 |
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 | 385 | 0.75 | 0.85 | 52 | empty |
| 2 | 70 | 0.60 | 0.90 | 17 | empty |
| 3 | 174 | 0.52 | 0.79 | 33 | empty |
| 4 | 96 | 0.35 | 0.74 | 19 | empty |
| 5 | 76 | 0.31 | 0.73 | 15 | 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 P25414
- Elsewhere: UniProt P25414 · AlphaFold DB P25414
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