Research workbench
Ap-2 clathrin adaptor alpha-appendage in complex with EPS15 dpf peptide
Analyse Ap-2 clathrin adaptor alpha-appendage in complex with EPS15 dpf peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1KYF
- Type
- protein
- Length
- 252 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-adaptin C; Epidermal growth factor receptor substrate 15
- UniProt
- P17427, P42567
- Pockets
- 2 · best druggability 0.40
Structure
x-ray diffraction · 2 distinct chains · 19% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-adaptin C | protein | 247 | 19% helix, 43% strand | P17427 |
| P | Epidermal growth factor receptor substrate 15 | protein | 5 | 0% helix, 0% strand | P42567 |
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 | 118 | 0.40 | 0.75 | 19 | empty |
| 2 | 64 | 0.34 | 0.77 | 16 | empty |
Interfaces
1 interface between chains.
- A–P · 275 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 1KYF · Ap-2 clathrin adaptor alpha-appendage in complex with EPS15 dpf peptide · the same entry in another collection · chain A against A, TM-score 1.00
- P17427 · AlphaFold monomer V2.0 prediction for ap-2 complex subunit alpha-2 (P17427) · a predicted model of the same protein · chain A against A, TM-score 0.96
- P42567 · AlphaFold monomer V2.0 prediction for epidermal growth factor receptor substrate 15… · a predicted model of the same protein · chain P against A, TM-score 0.91
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 P17427
- Every structure of UniProt P42567
- Elsewhere: RCSB PDB 1KYF · PDBe 1KYF · UniProt P17427 · UniProt P42567
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.