Research workbench
Structure of human SFPQ/PSPC1 heterodimer
Analyse Structure of human SFPQ/PSPC1 heterodimer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5WPA
- Type
- protein
- Length
- 479 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Splicing factor, proline- and glutamine-rich; Paraspeckle component 1
- UniProt
- P23246, Q8WXF1
- Pockets
- 5 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Splicing factor, proline- and glutamine-rich | protein | 224 | 38% helix, 24% strand | P23246 |
| B | Paraspeckle component 1 | protein | 255 | 40% helix, 20% strand | Q8WXF1 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 999 | 0.79 | 0.81 | 79 | empty |
| 2 | 203 | 0.46 | 0.74 | 28 | empty |
| 3 | 109 | 0.43 | 0.77 | 20 | empty |
| 4 | 144 | 0.39 | 0.74 | 18 | empty |
| 5 | 76 | 0.32 | 0.75 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 4254 Ų buried · 59 hydrogen bonds · protein-protein
Compared structures
- 5WPA · Structure of human SFPQ/PSPC1 heterodimer · the same entry in another collection · chain A against A, TM-score 1.00
- Q8WXF1 · AlphaFold monomer V2.0 prediction for paraspeckle component 1 (Q8WXF1) · a predicted model of the same protein · chain B against A, TM-score 0.94
- P23246 · AlphaFold monomer V2.0 prediction for splicing factor, proline- and glutamine-rich… · a predicted model of the same protein · chain A against A, TM-score 0.93
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 P23246
- Every structure of UniProt Q8WXF1
- Elsewhere: RCSB PDB 5WPA · PDBe 5WPA · UniProt P23246 · UniProt Q8WXF1
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