Structure of U2AF65 variant with BRU3C2 DNA

Structure

x-ray diffraction · 3 distinct chains · 24% helix, 32% strand (DSSP).

Ligands and binding sites

• CPQ · N,N-bis(3-D-gluconamidopropyl)deoxycholamide · ligand · chains B
• SO4 · Sulfate ion · ion · 7 copies · chains A, P, B
• DIO · 1,4-diethylene dioxide · additive · 6 copies · chains A, B
• GOL · Glycerol · additive · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Interfaces

4 interfaces between chains.

• B–E · 599 Ų buried · 15 hydrogen bonds · protein-nucleic
• A–P · 556 Ų buried · 15 hydrogen bonds · protein-nucleic
• B–P · 464 Ų buried · 6 hydrogen bonds · protein-nucleic
• A–B · 283 Ų buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (nucleotide modification).

Compared structures

• 3VAG · Structure of U2AF65 variant with BrU3C2 DNA · 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 0.54

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 3VAG · PDBe 3VAG · UniProt P26368