MolNFT v1 · #105307 · protein
A conserved phosphorylation switch controls the interaction between cadherin and beta-catenin in vitro and in vivo
4R11: “A conserved phosphorylation switch controls the interaction between cadherin and beta-catenin in vitro and in…”. X-ray diffraction. MolNFT v1 #105307 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4R11
- Type
- protein
- Length
- 1,701 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O44326, Q967F4
Structure
x-ray diffraction · 6 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 534 | — | O44326 |
| B | — | protein | 43 | — | Q967F4 |
| C | — | protein | 536 | — | O44326 |
| D | — | protein | 42 | — | Q967F4 |
| E | — | protein | 508 | — | O44326 |
| F | — | protein | 38 | — | Q967F4 |
Compared structures
- 4R11 · A conserved phosphorylation switch controls the interaction between cadherin and… · the same entry in another collection · chain F against F, TM-score 1.00
- O44326 · AlphaFold monomer V2.0 prediction for beta-catenin-like protein hmp-2 (O44326) · a predicted model of the same protein · chain C against A, TM-score 1.00
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 O44326
- Every structure of UniProt Q967F4
- Elsewhere: RCSB PDB 4R11 · PDBe 4R11 · UniProt O44326 · UniProt Q967F4
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