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Solution NMR structure of the protease-resistent domain of xenopus laevis EPABP2

Analyse Solution NMR structure of the protease-resistent domain of xenopus laevis EPABP2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2JWN
Type
protein
Length
248 residues
Chains
2
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Embryonic polyadenylate-binding protein 2-B
UniProt
Q6TY21
Pockets
1 · best druggability 0.70

Structure

solution nmr · 1 distinct chain · 21% helix, 26% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BEmbryonic polyadenylate-binding protein 2-Bprotein12421% helix, 26% strandQ6TY21

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14320.700.8147empty

Interfaces

1 interface between chains.

  • A–B · 1772 Ų buried · 26 hydrogen bonds · protein-protein

Compared structures

  • 2JWN · Solution NMR structure of the protease-resistent domain of Xenopus laevis ePABP2 · the same entry in another collection · chain A against A, TM-score 1.00
  • Q6TY21 · AlphaFold monomer V2.0 prediction for embryonic polyadenylate-binding protein 2-B (Q6TY21) · a predicted model of the same protein · chain B against A, TM-score 0.66

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