Research workbench
Solution structure of the complex of the ptb domain of snt-2 and 19- residue peptide (aa 1571-1589) of halk
Analyse Solution structure of the complex of the ptb domain of snt-2 and 19- residue… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2YS5
- Type
- protein
- Length
- 165 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fibroblast growth factor receptor substrate 3; ALK tyrosine kinase receptor
- EC
- 2.7.10.1
- UniProt
- O43559, Q9UM73
- Pockets
- 2 · best druggability 0.35
Structure
solution nmr · 2 distinct chains · 8% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fibroblast growth factor receptor substrate 3 | protein | 146 | 10% helix, 27% strand | O43559 |
| B | ALK tyrosine kinase receptor (EC 2.7.10.1) | protein | 19 | 0% helix, 11% strand | Q9UM73 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 60 | 0.35 | 0.78 | 19 | empty |
| 2 | 105 | 0.35 | 0.73 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 1249 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 2YS5 · Solution structure of the complex of the PTB domain of SNT-2 and 19-residue peptide (aa… · the same entry in another collection · chain A against A, TM-score 1.00
- O43559 · AlphaFold monomer V2.0 prediction for fibroblast growth factor receptor substrate 3… · a predicted model of the same protein · chain A against A, TM-score 0.71
- Q9UM73 · AlphaFold monomer V2.0 prediction for ALK tyrosine kinase receptor (Q9UM73) · a predicted model of the same protein · chain B against A, TM-score 0.19
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 O43559
- Every structure of UniProt Q9UM73
- Elsewhere: RCSB PDB 2YS5 · PDBe 2YS5 · UniProt O43559 · UniProt Q9UM73
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