Research workbench
AlphaFold monomer V2.0 prediction for ATP-dependent RNA helicase rhlb (Q7MGP7)
Analyse AlphaFold monomer V2.0 prediction for ATP-dependent RNA helicase rhlb (Q7MGP7) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q7MGP7
- Type
- protein
- Length
- 435 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7C348FbA4a15b2448ac5E3e6Ed52a64247E8F33f
- Molecule
- ATP-dependent RNA helicase rhlb
- UniProt
- Q7MGP7
- Pockets
- 3 · best druggability 0.76
Structure
1 distinct chain · 41% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent RNA helicase rhlb | protein | 435 | 41% helix, 15% strand | Q7MGP7 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 763 | 0.76 | 0.81 | 62 | empty |
| 2 | 113 | 0.42 | 0.77 | 19 | empty |
| 3 | 104 | 0.40 | 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 Q7MGP7
- Elsewhere: UniProt Q7MGP7 · AlphaFold DB Q7MGP7
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