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AlphaFold monomer V2.0 prediction for ATP-dependent RNA helicase MRH4, mitochondrial (A1CSR1)
Analyse AlphaFold monomer V2.0 prediction for ATP-dependent RNA helicase MRH4… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A1CSR1
- Type
- protein
- Length
- 632 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x77ced317A34D07425C0D730f27048EFb6B0c5E7C
- Molecule
- ATP-dependent RNA helicase MRH4, mitochondrial
- UniProt
- A1CSR1
- Pockets
- 7 · best druggability 0.75
Structure
1 distinct chain · 38% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent RNA helicase MRH4, mitochondrial | protein | 632 | 38% helix, 11% strand | A1CSR1 |
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 | 981 | 0.75 | 0.78 | 110 | empty |
| 2 | 94 | 0.48 | 0.81 | 27 | empty |
| 3 | 104 | 0.42 | 0.77 | 20 | empty |
| 4 | 109 | 0.40 | 0.76 | 19 | empty |
| 5 | 82 | 0.35 | 0.76 | 13 | 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 A1CSR1
- Elsewhere: UniProt A1CSR1 · AlphaFold DB A1CSR1
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