Research workbench
AlphaFold monomer V2.0 prediction for silencing boundary- establishment protein FUB1 (P25659)
Analyse AlphaFold monomer V2.0 prediction for silencing boundary- establishment protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P25659
- Type
- protein
- Length
- 250 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5881B09f2D8e743400698633641fc1cD2Ed2BE6F
- UniProt
- P25659
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 250 | — | P25659 |
Compared structures
- 7TEO · Cryo-EM structure of the 20S alpha 3 deletion proteasome core particle in complex with… · an experimental structure of the same protein · chain A against a, TM-score 0.12
- 7TEO · Cryo-EM structure of the 20S Alpha 3 Deletion proteasome core particle in complex with… · an experimental structure of the same protein · chain A against a, TM-score 0.12
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 P25659
- Elsewhere: UniProt P25659 · AlphaFold DB P25659
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