Research workbench
Structure of the EPS15-EH2 STONIN2 complex
Analyse Structure of the EPS15-EH2 STONIN2 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2JXC
- Type
- protein
- Length
- 135 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Epidermal growth factor receptor substrate 15; Stonin-2
- UniProt
- P42566, Q8WXE9
- Ligands
- CA
Structure
solution nmr · 2 distinct chains · 40% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Epidermal growth factor receptor substrate 15 | protein | 95 | 53% helix, 7% strand | P42566 |
| B | Stonin-2 | protein | 40 | 10% helix, 0% strand | Q8WXE9 |
Ligands and binding sites
- CA · Calcium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 1137 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 2JXC · Structure of the EPS15-EH2 Stonin2 Complex · the same entry in another collection · chain A against A, TM-score 1.00
- P42566 · 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 0.93
- Q8WXE9 · AlphaFold monomer V2.0 prediction for stonin-2 (Q8WXE9) · a predicted model of the same protein · chain B against A, TM-score 0.30
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 P42566
- Every structure of UniProt Q8WXE9
- Elsewhere: RCSB PDB 2JXC · PDBe 2JXC · UniProt P42566 · UniProt Q8WXE9
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.