Research workbench
AlphaFold monomer V2.0 prediction for proteasome assembly chaperone 1 (B0CM32)
Analyse AlphaFold monomer V2.0 prediction for proteasome assembly chaperone 1 (B0CM32) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B0CM32
- Type
- protein
- Length
- 290 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xaa53776A41fB2e67da75A96E8a53746b6874aAB4
- Molecule
- Proteasome assembly chaperone 1
- UniProt
- B0CM32
- Pockets
- 5 · best druggability 0.53
Structure
1 distinct chain · 33% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Proteasome assembly chaperone 1 | protein | 290 | 33% helix, 22% strand | B0CM32 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 259 | 0.53 | 0.76 | 26 | empty |
| 2 | 170 | 0.49 | 0.77 | 24 | empty |
| 3 | 76 | 0.47 | 0.83 | 16 | empty |
| 4 | 86 | 0.38 | 0.76 | 13 | empty |
| 5 | 54 | 0.28 | 0.75 | 9 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 B0CM32
- Elsewhere: UniProt B0CM32 · AlphaFold DB B0CM32
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