Research workbench
AlphaFold monomer V2.0 prediction for pre-mRNA-splicing factor ATP- dependent RNA helicase PRP16 (Q92620)
Analyse AlphaFold monomer V2.0 prediction for pre-mRNA-splicing factor ATP- dependent… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q92620
- Type
- protein
- Length
- 1,227 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x025f3b1a898b05AD2731bE6Ab72687b5920c4A3F
- Molecule
- Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP16
- UniProt
- Q92620
- Pockets
- 20 · best druggability 0.81
Structure
1 distinct chain · 37% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP16 | protein | 1227 | 37% helix, 11% strand | Q92620 |
Pockets
20 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 465 | 0.81 | 0.89 | 46 | empty |
| 2 | 229 | 0.71 | 0.87 | 41 | empty |
| 3 | 732 | 0.70 | 0.77 | 51 | empty |
| 4 | 184 | 0.65 | 0.85 | 30 | empty |
| 5 | 204 | 0.64 | 0.83 | 40 | empty |
Compared structures
- 7A5P · Human C Complex Spliceosome - Medium-resolution PERIPHERY · an experimental structure of the same protein · chain A against r, TM-score 0.46
- 7A5P · Human C complex spliceosome - medium-resolution periphery · an experimental structure of the same protein · chain A against r, TM-score 0.46
- 6ZYM · Human C complex spliceosome - high-resolution core · an experimental structure of the same protein · chain A against r, TM-score 0.03
- 6ZYM · Human C Complex Spliceosome - High-resolution CORE · an experimental structure of the same protein · chain A against r, TM-score 0.03
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 Q92620
- Elsewhere: UniProt Q92620 · AlphaFold DB Q92620
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