Crystal structure of the IMP3 and MPP10 complex

Structure

x-ray diffraction · 4 distinct chains · 59% helix, 6% strand (DSSP).

Ligands and binding sites

• SO4 · Sulfate ion · ion · 5 copies · chains A, B, U, V

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

Pockets

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

Interfaces

6 interfaces between chains.

• B–V · 1008 Ų buried · 4 hydrogen bonds · protein-protein
• A–U · 971 Ų buried · 6 hydrogen bonds · protein-protein
• A–V · 410 Ų buried · 3 hydrogen bonds · protein-protein
• A–B · 406 Ų buried · 7 hydrogen bonds · protein-protein
• U–V · 339 Ų buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 modified (engineered).

Compared structures

• 5WXM · Crystal structure of the Imp3 and Mpp10 complex · the same entry in another collection · chain V against V, TM-score 1.00
• P32899 · AlphaFold monomer V2.0 prediction for U3 small nucleolar ribonucleoprotein protein IMP3… · a predicted model of the same protein · chain B against A, TM-score 0.98
• P47083 · AlphaFold monomer V2.0 prediction for U3 small nucleolar RNA- associated protein MPP10… · a predicted model of the same protein · chain U against A, TM-score 0.79

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 P32899
• Every structure of UniProt P47083
• Elsewhere: RCSB PDB 5WXM · PDBe 5WXM · UniProt P32899 · UniProt P47083