Research workbench
AlphaFold monomer V2.0 prediction for ribulose bisphosphate carboxylase small subunit (Q31NB2)
Analyse AlphaFold monomer V2.0 prediction for ribulose bisphosphate carboxylase small… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q31NB2
- Type
- protein
- Length
- 111 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x83D41D67fBE58b08eAFC0b0e700399Bf4326f413
- Molecule
- Ribulose bisphosphate carboxylase small subunit
- UniProt
- Q31NB2
- Pockets
- 2 · best druggability 0.42
Structure
1 distinct chain · 24% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribulose bisphosphate carboxylase small subunit | protein | 111 | 24% helix, 23% strand | Q31NB2 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 68 | 0.42 | 0.80 | 15 | empty |
| 2 | 95 | 0.39 | 0.76 | 16 | empty |
Compared structures
- 6HBC · Structure of the repeat unit in the network formed by CcmM and Rubisco from Synechococcus… · an experimental structure of the same protein · chain A against D, TM-score 0.93
- 6HBC · Structure of the repeat unit in the network formed by ccmm and rubisco from synechococcus… · an experimental structure of the same protein · chain A against D, TM-score 0.93
- 8WPZ · Cryo-ET structure of RuBisCO at 3.9 angstroms from Synechococcus elongatus PCC 7942 · an experimental structure of the same protein · chain A against B, TM-score 0.87
- 8BCM · Structure of Synechococcus elongatus PCC 7942 Rubisco recombinantly expressed from E.coli · an experimental structure of the same protein · chain A against P, TM-score 0.87
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 Q31NB2
- Elsewhere: UniProt Q31NB2 · AlphaFold DB Q31NB2
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