Research workbench
AlphaFold monomer V2.0 prediction for pre-mRNA-splicing factor CWF10 (O94316)
Analyse AlphaFold monomer V2.0 prediction for pre-mRNA-splicing factor CWF10 (O94316) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- O94316
- Type
- protein
- Length
- 984 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xc0F878C3f3E2a1874e2A6daC80d429e553DdB0D5
- Molecule
- Pre-mRNA-splicing factor CWF10
- UniProt
- O94316
- Pockets
- 9 · best druggability 0.78
Structure
1 distinct chain · 35% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pre-mRNA-splicing factor CWF10 | protein | 984 | 35% helix, 21% strand | O94316 |
Pockets
9 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 108 | 0.78 | 0.98 | 25 | empty |
| 2 | 1103 | 0.75 | 0.78 | 85 | empty |
| 3 | 390 | 0.61 | 0.76 | 44 | empty |
| 4 | 272 | 0.60 | 0.79 | 27 | empty |
| 5 | 101 | 0.53 | 0.83 | 25 | empty |
Compared structures
- 9ESH · Structure of a B-state intermediate committed to discard (Bd-I state) · an experimental structure of the same protein · chain A against B, TM-score 0.92
- 9ESI · Structure of a B-state intermediate committed to discard (Bd-II state) · an experimental structure of the same protein · chain A against B, TM-score 0.92
- 3JB9 · Cryo-EM structure of the yeast spliceosome at 3.6 angstrom resolution · an experimental structure of the same protein · chain A against B, TM-score 0.90
- 3JB9 · Cryo-EM structure of the yeast spliceosome at 3.6 ångström resolution · an experimental structure of the same protein · chain A against B, TM-score 0.90
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 O94316
- Elsewhere: UniProt O94316 · AlphaFold DB O94316
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