MolNFT v1 · #333095 · protein
AlphaFold monomer V2.0 prediction for ribulose-1,5 bisphosphate CARBOXYLASE/OXYGENASE large subunit N-methyltransferase, chloroplastic (P94026)
P94026: “AlphaFold monomer V2.0 prediction for ribulose-1,5 bisphosphate CARBOXYLASE/OXYGENASE large subunit…”. 3 pockets (best druggability 0.75). MolNFT v1 #333095 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- P94026
- Type
- protein
- Length
- 491 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x493A46D594a1E8e8D0cF404bE2e0aEf46432960F
- Molecule
- Ribulose-1,5 bisphosphate CARBOXYLASE/OXYGENASE large subunit N-methyltransferase…
- UniProt
- P94026
- Pockets
- 3 · best druggability 0.75
Structure
1 distinct chain · 42% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribulose-1,5 bisphosphate CARBOXYLASE/OXYGENASE large subunit N-methyltransferase, chloroplastic | protein | 491 | 42% helix, 13% strand | P94026 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1121 | 0.75 | 0.77 | 119 | empty |
| 2 | 269 | 0.56 | 0.77 | 38 | empty |
| 3 | 69 | 0.30 | 0.74 | 19 | 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 P94026
- Elsewhere: UniProt P94026 · AlphaFold DB P94026
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