Research workbench
Human splicing factor, construct 3
Analyse Human splicing factor, construct 3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4WII
- Type
- protein
- Length
- 498 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Splicing factor, proline- and glutamine-rich
- UniProt
- P23246
- Ligands
- SO4
- Pockets
- 6 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Splicing factor, proline- and glutamine-rich | protein | 253 | 42% helix, 20% strand | P23246 |
| B | Splicing factor, proline- and glutamine-rich | protein | 245 | 40% helix, 22% strand | P23246 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1058 | 0.76 | 0.78 | 60 | EDO |
| 2 | 331 | 0.66 | 0.81 | 29 | empty |
| 3 | 370 | 0.66 | 0.80 | 32 | empty |
| 4 | 143 | 0.41 | 0.74 | 22 | empty |
| 5 | 122 | 0.36 | 0.73 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 4956 Ų buried · 80 hydrogen bonds · protein-protein
Compared structures
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
- Elsewhere: RCSB PDB 4WII · PDBe 4WII · UniProt P23246
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