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Crystal structure of human dead-box RNA helicase DDX21 in complex with AMP

Analyse Crystal structure of human dead-box RNA helicase DDX21 in complex with AMP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6L5M
Type
protein
Length
1,830 residues
Chains
5
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Nucleolar RNA helicase 2
EC
3.6.4.13
UniProt
Q9NR30
Ligands
AMP
Pockets
20 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, ENucleolar RNA helicase 2 (EC 3.6.4.13)protein36641% helix, 17% strandQ9NR30

Ligands and binding sites

  • AMP · Adenosine monophosphate · ligand · 5 copies · chains A, B, C, D, E

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18220.710.7681AMP
23210.550.7539empty
33400.550.7546empty
42110.500.7629empty
52150.490.7526empty

Interfaces

6 interfaces between chains.

  • B–C · 583 Ų buried · 1 hydrogen bond · protein-protein
  • D–E · 541 Ų buried · 3 hydrogen bonds · protein-protein
  • A–B · 516 Ų buried · 1 hydrogen bond · protein-protein
  • C–D · 467 Ų buried · 2 hydrogen bonds · protein-protein
  • A–C · 185 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 6L5M · Crystal structure of human DEAD-box RNA helicase DDX21 in complex with AMP · the same entry in another collection · chain E against E, TM-score 1.00
  • Q9NR30 · AlphaFold monomer V2.0 prediction for nucleolar RNA helicase 2 (Q9NR30) · a predicted model of the same protein · chain E against A, TM-score 0.58

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