Research workbench
Structure, phosphorylation and U2AF65 binding of the Nterminal Domain of splicing factor 1 during 3 splice site Recognition
Analyse Structure, phosphorylation and U2AF65 binding of the Nterminal Domain of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2M0G
- Type
- protein
- Length
- 249 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- NOT
- Source
- Homo sapiens
- Molecule
- Splicing factor 1; Splicing factor U2AF 65 kDa subunit
- UniProt
- Q15637, P26368
- Pockets
- 2 · best druggability 0.64
Structure
solution nmr · resolution NOT · 2 distinct chains · 31% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Splicing factor 1 | protein | 145 | 31% helix, 0% strand | Q15637 |
| B | Splicing factor U2AF 65 kDa subunit | protein | 104 | 30% helix, 20% strand | P26368 |
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 543 | 0.64 | 0.76 | 49 | empty |
| 2 | 115 | 0.51 | 0.81 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 1371 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 2M0G · Structure, phosphorylation and U2AF65 binding of the nterminal domain of splicing factor… · 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 B against A, TM-score 0.89
- Q15637 · AlphaFold monomer V2.0 prediction for splicing factor 1 (Q15637) · a predicted model of the same protein · chain A against A, TM-score 0.59
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 Q15637
- Every structure of UniProt P26368
- Elsewhere: RCSB PDB 2M0G · PDBe 2M0G · UniProt Q15637 · UniProt P26368
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