Research workbench
Structure IV of intact U2AF65 recognizing the 3' splice site signal
Analyse Structure IV of intact U2AF65 recognizing the 3' splice site signal in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5EV4
- Type
- protein + RNA
- Length
- 206 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Splicing factor U2AF 65 kda subunit; DNA/RNA (5'-R(P*UP*UP*UP*(UD)P*UP*U)-D(P*(BRU)P*(UD))…
- UniProt
- P26368
- Pockets
- 1 · best druggability 0.28
Structure
x-ray diffraction · 2 distinct chains · 25% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Splicing factor U2AF 65 kda subunit | protein | 197 | 25% helix, 28% strand | P26368 |
| B | DNA/RNA (5'-R(P*UP*UP*UP*(UD)P*UP*U)-D(P*(BRU)P*(UD))- R(P*C)-3') | rna | 9 | — | — |
Ligands and binding sites
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 64 | 0.28 | 0.73 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 1342 Ų buried · 49 hydrogen bonds · protein-nucleic
Modifications
Observed in the structure: 1 modified (nucleotide modification).
Compared structures
- 5EV4 · Structure IV of Intact U2AF65 Recognizing the 3' Splice Site Signal · the same entry in another collection · chain A against A, TM-score 1.00
- P26368 · AlphaFold monomer V2.0 prediction for splicing factor U2AF 65 kda subunit (P26368) · a predicted model of the same protein · chain A against A, TM-score 0.83
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 P26368
- Elsewhere: RCSB PDB 5EV4 · PDBe 5EV4 · UniProt P26368
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