MolNFT v1 · #6962 · protein
Structural basis of the recognition of the dishevelled dep domain in the wnt signaling pathway
1FSH: “Structural basis of the recognition of the dishevelled dep domain in the wnt signaling pathway”. Solution nmr. MolNFT v1 #6962 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1FSH
- Type
- protein
- Length
- 94 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P51141
Structure
solution nmr · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 94 | — | P51141 |
Compared structures
- 1FSH · Structural basis of the recognition of the dishevelled dep domain in the wnt signaling… · the same entry in another collection · chain A against A, TM-score 1.00
- P51141 · AlphaFold monomer V2.0 prediction for segment polarity protein dishevelled homolog dvl-1… · a predicted model of the same protein · chain A against A, TM-score 0.75
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 P51141
- Elsewhere: RCSB PDB 1FSH · PDBe 1FSH · UniProt P51141
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