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Crystal structure (II) of nova-1 KH1/KH2 domain tandem with 25NT RNA hairpin

Analyse Crystal structure (II) of nova-1 KH1/KH2 domain tandem with 25NT RNA hairpin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2ANR
Type
protein + RNA
Length
180 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
5'-R(*CP*(5BU) P*CP*GP*CP*GP*GP*AP*UP*CP*AP*GP*UP*CP*AP*CP*CP*CP*AP*AP*GP*CP*GP*AP*G…
UniProt
P51513
Ligands
MG, K
Pockets
2 · best druggability 0.34

Structure

x-ray diffraction · 2 distinct chains · 49% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
B5'-R(*CP*(5BU) P*CP*GP*CP*GP*GP*AP*UP*CP*AP*GP*UP*CP*AP*CP*CP*CP*AP*AP*GP*CP*GP*AP*G )-3'rna25——
ANeuro-oncological ventral antigen 1protein15549% helix, 25% strandP51513

Ligands and binding sites

  • MG · Magnesium ion · metal · 2 copies · chains B
  • K · Potassium ion · metal · chains B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1660.340.7613empty
2720.280.7411K, MG

Interfaces

1 interface between chains.

  • B–A · 620 Ų buried · 16 hydrogen bonds · protein-nucleic

Modifications

Observed in the structure: 3 modified (engineered, nucleotide modification).

Compared structures

  • 2ANR · Crystal structure (II) of Nova-1 KH1/KH2 domain tandem with 25nt RNA hairpin · the same entry in another collection · chain B against B, TM-score 1.00
  • P51513 · AlphaFold monomer V2.0 prediction for RNA-binding protein nova-1 (P51513) · a predicted model of the same protein · chain A against A, TM-score 0.98

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