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Crystal structure of the PRP43-ADP-BEF3-U7-RNA complex

Analyse Crystal structure of the PRP43-ADP-BEF3-U7-RNA complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5LTA
Type
protein + RNA
Length
705 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP43; RNA…
EC
3.6.4.13
UniProt
G0RY84
Ligands
ADP, BEF, MG
Pockets
9 · best druggability 0.86

Structure

x-ray diffraction · 2 distinct chains · 42% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APre-mRNA-splicing factor ATP-dependent RNA helicase PRP43 (EC 3.6.4.13)protein69842% helix, 18% strandG0RY84
ERNA (5'-R(P*UP*UP*UP*UP*UP*UP*UP*U)-3')rna7——

Ligands and binding sites

  • ADP · Adenosine-5'-diphosphate · ligand · chains A
  • BEF · Beryllium trifluoride ion · ligand · chains A
  • MG · Magnesium ion · metal · chains A
  • CAC · Cacodylate ion · additive · chains A

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

Pockets

9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111640.860.87101empty
22040.670.8527empty
32770.640.8137ADP, MG, BEF
42960.600.7938empty
51430.390.7424empty

Interfaces

1 interface between chains.

  • A–E · 1126 Ų buried · 18 hydrogen bonds · protein-nucleic

Compared structures

  • 5LTA · Crystal structure of the Prp43-ADP-BeF3-U7-RNA complex · the same entry in another collection · chain A against A, TM-score 1.00

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