Research workbench
Structure of yeast U2AF complex
Analyse Structure of yeast U2AF complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4YH8
- Type
- protein
- Length
- 235 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Splicing factor U2AF 23 kda subunit; Splicing factor U2AF 59 kda subunit
- UniProt
- Q09176, P36629
- Ligands
- ZN
- Pockets
- 3 · best druggability 0.62
Structure
x-ray diffraction · 2 distinct chains · 42% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Splicing factor U2AF 23 kda subunit | protein | 180 | 44% helix, 16% strand | Q09176 |
| B | Splicing factor U2AF 59 kda subunit | protein | 55 | 36% helix, 2% strand | P36629 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 210 | 0.62 | 0.82 | 27 | empty |
| 2 | 171 | 0.46 | 0.75 | 20 | empty |
| 3 | 70 | 0.35 | 0.76 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 1727 Ų buried · 25 hydrogen bonds · protein-protein
Compared structures
- 4YH8 · Structure of yeast U2AF complex · the same entry in another collection · chain A against A, TM-score 1.00
- Q09176 · AlphaFold monomer V2.0 prediction for splicing factor U2AF 23 kda subunit (Q09176) · a predicted model of the same protein · chain A against A, TM-score 0.98
- P36629 · AlphaFold monomer V2.0 prediction for splicing factor U2AF 59 kda subunit (P36629) · a predicted model of the same protein · chain B against A, TM-score 0.51
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 Q09176
- Every structure of UniProt P36629
- Elsewhere: RCSB PDB 4YH8 · PDBe 4YH8 · UniProt Q09176 · UniProt P36629
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