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Two different open conformations of the helicase core of the RNA helicase hera

Analyse Two different open conformations of the helicase core of the RNA helicase hera in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4KBF
Type
protein
Length
730 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Heat resistant RNA dependent ATPase
UniProt
Q72GF3
Ligands
AMP, NA, SO4
Pockets
4 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BHeat resistant RNA dependent ATPaseprotein36541% helix, 18% strandQ72GF3

Ligands and binding sites

  • AMP · Adenosine monophosphate · ligand · chains A
  • NA · Sodium ion · metal · 2 copies · chains A
  • SO4 · Sulfate ion · ion · chains B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15490.690.7958empty
21790.490.7728empty
3740.370.7820empty
41050.330.7214empty

Interfaces

1 interface between chains.

  • A–B · 993 Ų buried · 9 hydrogen bonds · protein-protein

Compared structures

  • 4KBF · two different open conformations of the helicase core of the RNA helicase Hera · the same entry in another collection · chain A against A, TM-score 1.00

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