Research workbench
Structure of phosphorylated SF1 complex with U2AF65-uhm domain
Analyse Structure of phosphorylated SF1 complex with U2AF65-uhm domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4FXW
- Type
- protein
- Length
- 417 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P26368, Q15637
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 105 | — | P26368 |
| B | — | protein | 101 | — | Q15637 |
| C | — | protein | 104 | — | P26368 |
| D | — | protein | 107 | — | Q15637 |
Compared structures
- 4FXW · Structure of phosphorylated SF1 complex with U2AF65-UHM domain · the same entry in another collection · chain D against D, 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 C against A, TM-score 0.96
- Q15637 · AlphaFold monomer V2.0 prediction for splicing factor 1 (Q15637) · a predicted model of the same protein · chain D against A, TM-score 0.88
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
- Every structure of UniProt Q15637
- Elsewhere: RCSB PDB 4FXW · PDBe 4FXW · UniProt P26368 · UniProt Q15637
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