Research workbench
AlphaFold monomer V2.0 prediction for H/ACA ribonucleoprotein complex subunit 2 (Q5RC65)
Analyse AlphaFold monomer V2.0 prediction for H/ACA ribonucleoprotein complex subunit 2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5RC65
- Type
- protein
- Length
- 153 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x1845261721C30faB0573FB733392972cFfDf9A53
- Molecule
- H/ACA ribonucleoprotein complex subunit 2
- UniProt
- Q5RC65
- Pockets
- 1 · best druggability 0.37
Structure
1 distinct chain · 41% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | H/ACA ribonucleoprotein complex subunit 2 | protein | 153 | 41% helix, 11% strand | Q5RC65 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 105 | 0.37 | 0.75 | 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 Q5RC65
- Elsewhere: UniProt Q5RC65 · AlphaFold DB Q5RC65
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