Research workbench
AlphaFold monomer V2.0 prediction for pre-mRNA-splicing ATP-dependent RNA helicase PRP28 (P23394)
Analyse AlphaFold monomer V2.0 prediction for pre-mRNA-splicing ATP-dependent RNA… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P23394
- Type
- protein
- Length
- 588 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4eB83b6340c032CC7AcdbC262D37E9627F422205
- Molecule
- Pre-mRNA-splicing ATP-dependent RNA helicase PRP28
- UniProt
- P23394
- Pockets
- 3 · best druggability 0.74
Structure
1 distinct chain · 40% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pre-mRNA-splicing ATP-dependent RNA helicase PRP28 | protein | 588 | 40% helix, 12% strand | P23394 |
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 | 875 | 0.74 | 0.78 | 86 | empty |
| 2 | 56 | 0.49 | 0.86 | 19 | empty |
| 3 | 114 | 0.42 | 0.77 | 14 | empty |
Compared structures
- 4W7S · Crystal structure of the yeast DEAD-box splicing factor Prp28 at 2.54 Angstroms resolution · an experimental structure of the same protein · chain A against A, TM-score 0.52
- 4W7S · Crystal structure of the yeast dead-box splicing factor PRP28 at 2.54 ångströms resolution · an experimental structure of the same protein · chain A against A, TM-score 0.52
- 5ZWN · Cryo-EM structure of the yeast pre-B complex at an average resolution of 3.3 ångström… · an experimental structure of the same protein · chain A against y, TM-score 0.39
- 5ZWN · Cryo-EM structure of the yeast pre-B complex at an average resolution of 3.3 angstrom… · an experimental structure of the same protein · chain A against y, TM-score 0.39
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 P23394
- Elsewhere: UniProt P23394 · AlphaFold DB P23394
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