Research workbench
AlphaFold monomer V2.0 prediction for RNA polymerase-associated protein rapa (A1RFP5)
Analyse AlphaFold monomer V2.0 prediction for RNA polymerase-associated protein rapa… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A1RFP5
- Type
- protein
- Length
- 968 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x04362FE85E29D99f21630583f4F3B6E962DCb76C
- Molecule
- RNA polymerase-associated protein rapa
- UniProt
- A1RFP5
- Pockets
- 17 · best druggability 0.73
Structure
1 distinct chain · 47% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RNA polymerase-associated protein rapa | protein | 968 | 47% helix, 18% strand | A1RFP5 |
Pockets
17 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 549 | 0.73 | 0.81 | 50 | empty |
| 2 | 544 | 0.65 | 0.76 | 55 | empty |
| 3 | 54 | 0.64 | 0.94 | 18 | empty |
| 4 | 151 | 0.64 | 0.86 | 28 | empty |
| 5 | 378 | 0.63 | 0.78 | 42 | 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 A1RFP5
- Elsewhere: UniProt A1RFP5 · AlphaFold DB A1RFP5
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