Research workbench
A conserved phosphorylation switch controls the interaction between cadherin and beta-catenin in vitro and in vivo
Analyse A conserved phosphorylation switch controls the interaction between cadherin… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4R10
- Type
- protein
- Length
- 579 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein humpback-2; Cadherin-related hmr-1
- UniProt
- O44326, Q967F4
- Ligands
- SO4
- Pockets
- 4 · best druggability 0.66
Structure
x-ray diffraction · 2 distinct chains · 70% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein humpback-2 | protein | 537 | 73% helix, 1% strand | O44326 |
| B | Cadherin-related hmr-1 | protein | 42 | 36% helix, 19% strand | Q967F4 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 211 | 0.66 | 0.84 | 35 | empty |
| 2 | 86 | 0.40 | 0.78 | 21 | empty |
| 3 | 52 | 0.36 | 0.79 | 10 | empty |
| 4 | 50 | 0.27 | 0.75 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 1871 Ų buried · 37 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (phosphorylation).
Compared structures
- 4R10 · A conserved phosphorylation switch controls the interaction between cadherin and… · the same entry in another collection · chain A against A, 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 A 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 4R10 · PDBe 4R10 · UniProt O44326 · UniProt Q967F4
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