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Crystal structure of a chimera of beta-catenin and alpha- catenin

Analyse Crystal structure of a chimera of beta-catenin and alpha- catenin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1DOW
Type
protein
Length
237 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Alpha-catenin; Beta-catenin
UniProt
P26231, Q02248
Pockets
1 · best druggability 0.53

Structure

x-ray diffraction · 2 distinct chains · 85% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAlpha-cateninprotein20588% helix, 0% strandP26231
BBeta-cateninprotein3266% helix, 0% strandQ02248

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11470.530.8021empty

Interfaces

1 interface between chains.

  • A–B · 1342 Ų buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 modified (engineered).

Compared structures

  • 1DOW · Crystal structure of a chimera of beta-catenin and alpha-catenin · the same entry in another collection · chain A against A, TM-score 1.00
  • P26231 · AlphaFold monomer V2.0 prediction for catenin alpha-1 (P26231) · a predicted model of the same protein · chain A against A, TM-score 0.97
  • Q02248 · AlphaFold monomer V2.0 prediction for catenin beta-1 (Q02248) · a predicted model of the same protein · chain B against A, TM-score 0.73

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