GL1X · GenesisL1 explorer

Research workbench

Crystal structure of beta-CATENIN/ICAT helical DOMAIN/UNPHOSPHORYLATED apc R3

Analyse Crystal structure of beta-CATENIN/ICAT helical DOMAIN/UNPHOSPHORYLATED apc R3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1T08
Type
protein
Length
571 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Beta-catenin; Beta-catenin-interacting protein 1; Adenomatous polyposis COLI protein
UniProt
P35222, Q9NSA3, P25054
Pockets
2 · best druggability 0.54

Structure

x-ray diffraction · 3 distinct chains · 73% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ABeta-cateninprotein51075% helix, 0% strandP35222
BBeta-catenin-interacting protein 1protein4676% helix, 0% strandQ9NSA3
CAdenomatous polyposis COLI proteinprotein150% helix, 0% strandP25054

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12070.540.7834empty
2510.290.7516empty

Interfaces

2 interfaces between chains.

  • A–C · 961 Ų buried · 21 hydrogen bonds · protein-protein
  • A–B · 676 Ų buried · 6 hydrogen bonds · protein-protein

Compared structures

  • 1T08 · Crystal structure of beta-catenin/ICAT helical domain/unphosphorylated APC R3 · the same entry in another collection · chain A against A, TM-score 1.00
  • P35222 · AlphaFold monomer V2.0 prediction for catenin beta-1 (P35222) · a predicted model of the same protein · chain A against A, TM-score 0.98
  • Q9NSA3 · AlphaFold monomer V2.0 prediction for beta-catenin-interacting protein 1 (Q9NSA3) · a predicted model of the same protein · chain B against A, TM-score 0.93

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.