GL1X · GenesisL1 explorer

Research workbench

Crystal structure of the core domain of RNA helicase DDX17 with RNA pri-125A-OLIGO1

Analyse Crystal structure of the core domain of RNA helicase DDX17 with RNA… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6UV2
Type
protein + RNA
Length
438 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Probable ATP-dependent RNA helicase DDX17; RNA 125A_OLIGO1
EC
3.6.4.13
UniProt
Q92841
Ligands
ADP, BEF, MG
Pockets
3 · best druggability 0.64

Structure

x-ray diffraction · 2 distinct chains · 42% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProbable ATP-dependent RNA helicase DDX17 (EC 3.6.4.13)protein43142% helix, 15% strandQ92841
CRNA 125A_OLIGO1rna7——

Ligands and binding sites

  • ADP · Adenosine-5'-diphosphate · ligand · chains A
  • BEF · Beryllium trifluoride ion · ligand · chains A
  • MG · Magnesium ion · metal · 4 copies · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13980.640.7954ADP, BEF, MG
21260.470.7921empty
3640.400.8022MG

Interfaces

1 interface between chains.

  • A–C · 782 Ų buried · 34 hydrogen bonds · protein-nucleic

Compared structures

  • 6UV2 · Crystal structure of the core domain of RNA helicase DDX17 with RNA pri-125a-oligo1 · the same entry in another collection · chain A against A, TM-score 1.00
  • Q92841 · AlphaFold monomer V2.0 prediction for probable ATP-dependent RNA helicase DDX17 (Q92841) · a predicted model of the same protein · chain A against A, TM-score 1.00

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.