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IMP1 KH1 and KH2 domains create a structural platform with unique RNA recognition and re-modelling properties

Analyse IMP1 KH1 and KH2 domains create a structural platform with unique RNA… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6QEY
Type
protein
Length
170 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Insulin-like growth factor 2 mRNA-binding protein 1
UniProt
Q9NZI8
Ligands
CCN, PO4
Pockets
1 · best druggability 0.27

Structure

x-ray diffraction · 1 distinct chain · 56% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AInsulin-like growth factor 2 mRNA-binding protein 1protein17056% helix, 22% strandQ9NZI8

Ligands and binding sites

  • CCN · Acetonitrile · ligand · chains A
  • PO4 · Phosphate ion · ion · 2 copies · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1530.270.7422empty

Compared structures

  • 6QEY · IMP1 KH1 and KH2 domains create a structural platform with unique RNA recognition and… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9NZI8 · AlphaFold monomer V2.0 prediction for insulin-like growth factor 2 mRNA-binding protein 1… · a predicted model of the same protein · chain A against A, TM-score 0.93

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