Research workbench
AlphaFold monomer V2.0 prediction for sumo-activating enzyme subunit 1B-2 (P0DI13)
Analyse AlphaFold monomer V2.0 prediction for sumo-activating enzyme subunit 1B-2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P0DI13
- Type
- protein
- Length
- 320 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5881B09f2D8e743400698633641fc1cD2Ed2BE6F
- Molecule
- Sumo-activating enzyme subunit 1B-2
- UniProt
- P0DI13
- Pockets
- 4 · best druggability 0.42
Structure
1 distinct chain · 43% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sumo-activating enzyme subunit 1B-2 | protein | 320 | 43% helix, 21% strand | P0DI13 |
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 107 | 0.42 | 0.77 | 16 | empty |
| 2 | 69 | 0.40 | 0.80 | 17 | empty |
| 3 | 99 | 0.40 | 0.76 | 18 | empty |
| 4 | 92 | 0.37 | 0.76 | 17 | 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 P0DI13
- Elsewhere: UniProt P0DI13 · AlphaFold DB P0DI13
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