Research workbench
Structural and thermodynamic characterization of cadherin-beta- catenin-alpha-catenin complex formation
Analyse Structural and thermodynamic characterization of cadherin-beta… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4ONS
- Type
- protein
- Length
- 552 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q61301, Q02248
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 230 | — | Q61301 |
| B | — | protein | 56 | — | Q02248 |
| C | — | protein | 205 | — | Q61301 |
| D | — | protein | 61 | — | Q02248 |
Compared structures
- 4ONS · Structural and thermodynamic characterization of cadherin-beta-catenin-alpha-catenin… · the same entry in another collection · chain D against D, TM-score 1.00
- Q02248 · AlphaFold monomer V2.0 prediction for catenin beta-1 (Q02248) · a predicted model of the same protein · chain D against A, TM-score 0.83
- Q61301 · AlphaFold monomer V2.0 prediction for catenin alpha-2 (Q61301) · a predicted model of the same protein · chain C against A, TM-score 0.80
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q61301
- Every structure of UniProt Q02248
- Elsewhere: RCSB PDB 4ONS · PDBe 4ONS · UniProt Q61301 · UniProt Q02248
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