Research workbench
AlphaFold monomer V2.0 prediction for SIT4-associating protein SAP155 (P43612)
Analyse AlphaFold monomer V2.0 prediction for SIT4-associating protein SAP155 (P43612) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P43612
- Type
- protein
- Length
- 1,002 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7a1388B6Aad67B04634A32f63b8A6D6005eab86c
- Molecule
- SIT4-associating protein SAP155
- UniProt
- P43612
- Pockets
- 9 · best druggability 0.64
Structure
1 distinct chain · 45% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SIT4-associating protein SAP155 | protein | 1002 | 45% helix, 2% strand | P43612 |
Pockets
9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 345 | 0.64 | 0.79 | 45 | empty |
| 2 | 390 | 0.59 | 0.76 | 41 | empty |
| 3 | 291 | 0.56 | 0.76 | 30 | empty |
| 4 | 246 | 0.53 | 0.76 | 27 | empty |
| 5 | 116 | 0.47 | 0.79 | 15 | 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 P43612
- Elsewhere: UniProt P43612 · AlphaFold DB P43612
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