Research workbench
Shc ptb domain complexed with a trka receptor phosphopeptide, NMR, minimized average structure
Analyse Shc ptb domain complexed with a trka receptor phosphopeptide, NMR, minimized… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1SHC
- Type
- protein
- Length
- 207 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Shc; Trka receptor phosphopeptide
- UniProt
- P29353, P04629
- Pockets
- 3 · best druggability 0.76
Structure
solution nmr · 2 distinct chains · 17% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Shc | protein | 195 | 18% helix, 29% strand | P29353 |
| B | Trka receptor phosphopeptide | protein | 12 | 0% helix, 0% strand | P04629 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 101 | 0.76 | 0.96 | 30 | empty |
| 2 | 135 | 0.41 | 0.75 | 23 | empty |
| 3 | 96 | 0.38 | 0.75 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 917 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (phosphorylation).
Compared structures
- 1SHC · Shc ptb domain complexed with a trka receptor phosphopeptide, NMR, minimized average… · the same entry in another collection · chain A against A, TM-score 1.00
- P29353 · AlphaFold monomer V2.0 prediction for shc-transforming protein 1 (P29353) · a predicted model of the same protein · chain A against A, TM-score 0.69
- P04629 · AlphaFold monomer V2.0 prediction for high affinity nerve growth factor receptor (P04629) · a predicted model of the same protein · chain B against A, TM-score 0.35
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 P29353
- Every structure of UniProt P04629
- Elsewhere: RCSB PDB 1SHC · PDBe 1SHC · UniProt P29353 · UniProt P04629
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