MolNFT v1 · #13002 · protein
Ap-2 clathrin adaptor alpha-appendage in complex with epsin dpw peptide
1KY6 · Alpha-adaptin C: “Ap-2 clathrin adaptor alpha-appendage in complex with epsin dpw peptide”. X-ray diffraction, 1 ligand (SO4), 3 pockets (best druggability 0.34). MolNFT v1 #13002 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1KY6
- Type
- protein
- Length
- 254 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-adaptin C; Eh domain binding protein epsin
- UniProt
- P17427, O88339
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.34
Structure
x-ray diffraction · 2 distinct chains · 19% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-adaptin C | protein | 247 | 19% helix, 43% strand | P17427 |
| P | Eh domain binding protein epsin | protein | 7 | 0% helix, 0% strand | O88339 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A, P
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 72 | 0.34 | 0.76 | 17 | empty |
| 2 | 62 | 0.31 | 0.75 | 12 | empty |
| 3 | 68 | 0.29 | 0.74 | 14 | empty |
Interfaces
1 interface between chains.
- A–P · 399 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 1KY6 · Ap-2 clathrin adaptor alpha-appendage in complex with epsin dpw 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
- O88339 · AlphaFold monomer V2.0 prediction for epsin-1 (O88339) · a predicted model of the same protein · chain P against A, TM-score 0.64
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 O88339
- Elsewhere: RCSB PDB 1KY6 · PDBe 1KY6 · UniProt P17427 · UniProt O88339
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