MolNFT v1 · #123588 · protein
FCHO1 mu homology domain (danio rerio) with bound EPS15 peptide
5JP2 · Epidermal growth factor receptor substrate 15: “FCHO1 mu homology domain (danio rerio) with bound EPS15 peptide”. X-ray diffraction, 1 ligand (ZN), 1 pocket (best druggability 0.73). MolNFT v1 #123588 on GenesisL1: 3D structure…
- PDB
- 5JP2
- Type
- protein
- Length
- 578 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Epidermal growth factor receptor substrate 15; F-bar domain only protein 1
- UniProt
- P42566, A0A0R4IJ14
- Ligands
- ZN
- Pockets
- 1 · best druggability 0.73
Structure
x-ray diffraction · 3 distinct chains · 10% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E, F | Epidermal growth factor receptor substrate 15 | protein | 18 | 0% helix, 0% strand | P42566 |
| A | F-bar domain only protein 1 | protein | 272 | 10% helix, 53% strand | A0A0R4IJ14 |
| B | F-bar domain only protein 1 | protein | 270 | 10% helix, 54% strand | A0A0R4IJ14 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 954 | 0.73 | 0.77 | 99 | empty |
Interfaces
3 interfaces between chains.
- E–A · 850 Ų buried · 10 hydrogen bonds · protein-protein
- F–B · 841 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 464 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 5JP2 · Fcho1 Mu homology domain (Danio Rerio) with bound Eps15 peptide · the same entry in another collection · chain E against E, 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 F against A, TM-score 0.22
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 A0A0R4IJ14
- Elsewhere: RCSB PDB 5JP2 · PDBe 5JP2 · UniProt P42566 · UniProt A0A0R4IJ14
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