Research workbench
AlphaFold monomer V2.0 prediction for histone chaperone RTT106 (A2RBA1)
Analyse AlphaFold monomer V2.0 prediction for histone chaperone RTT106 (A2RBA1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A2RBA1
- Type
- protein
- Length
- 458 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd10960F956646DE8b64d3598984c91C2d5Af3D7b
- Molecule
- Histone chaperone RTT106
- UniProt
- A2RBA1
- Pockets
- 7 · best druggability 0.53
Structure
1 distinct chain · 21% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone chaperone RTT106 | protein | 458 | 21% helix, 23% strand | A2RBA1 |
Pockets
7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 256 | 0.53 | 0.76 | 26 | empty |
| 2 | 141 | 0.42 | 0.75 | 18 | empty |
| 3 | 78 | 0.38 | 0.78 | 19 | empty |
| 4 | 112 | 0.36 | 0.73 | 18 | empty |
| 5 | 52 | 0.31 | 0.77 | 15 | 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 A2RBA1
- Elsewhere: UniProt A2RBA1 · AlphaFold DB A2RBA1
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