Research workbench
Solution structure of the apo EH1 domain of mouse epidermal growth factor receptor substrate 15, EPS15
Analyse Solution structure of the apo EH1 domain of mouse epidermal growth factor… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QJT
- Type
- protein
- Length
- 99 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Epidermal growth factor receptor substrate substrate 15, EPS15
- UniProt
- P42567
- Pockets
- 1 · best druggability 0.31
Structure
solution nmr · 1 distinct chain · 48% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Epidermal growth factor receptor substrate substrate 15, EPS15 | protein | 99 | 48% helix, 0% strand | P42567 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 68 | 0.31 | 0.74 | 16 | empty |
Compared structures
- 1QJT · Solution structure of the apo EH1 domain of mouse epidermal growth factor receptor… · the same entry in another collection · chain A against A, TM-score 1.00
- P42567 · AlphaFold monomer V2.0 prediction for epidermal growth factor receptor substrate 15… · a predicted model of the same protein · chain A against A, TM-score 0.79
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 P42567
- Elsewhere: RCSB PDB 1QJT · PDBe 1QJT · UniProt P42567
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