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Crystal structure of full-length mouse alphae-catenin

Analyse Crystal structure of full-length mouse alphae-catenin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4K1N
Type
protein
Length
1,040 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Catenin alpha-1
UniProt
P26231
Pockets
11 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 78% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BCatenin alpha-1protein52078% helix, 0% strandP26231

Pockets

11 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17250.790.83102empty
25890.730.8172empty
32150.650.8442empty
4990.620.8821empty
55100.610.7546empty

Interfaces

1 interface between chains.

  • A–B · 1477 Ų buried · 6 hydrogen bonds · protein-protein

Compared structures

  • 4K1N · Crystal structure of full-length mouse alphaE-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 0.87

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