Research workbench
MU2 adaptin subunit (AP50) of AP2 adaptor (second domain), complexed with non-canonical internalization peptide vedyeqglsg
Analyse MU2 adaptin subunit (AP50) of AP2 adaptor (second domain), complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2BP5
- Type
- protein
- Length
- 263 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Clathrin coat assembly protein AP50; P2X purinoceptor 4
- UniProt
- P84092, P51577
- Pockets
- 2 · best druggability 0.44
Structure
x-ray diffraction · 2 distinct chains · 2% helix, 56% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| M | Clathrin coat assembly protein AP50 | protein | 253 | 2% helix, 57% strand | P84092 |
| P | P2X purinoceptor 4 | protein | 10 | 0% helix, 20% strand | P51577 |
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 | 150 | 0.44 | 0.75 | 24 | empty |
| 2 | 104 | 0.38 | 0.75 | 20 | empty |
Interfaces
1 interface between chains.
- M–P · 723 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 2BP5 · MU2 adaptin subunit (AP50) of AP2 adaptor (second domain), complexed with non-canonical… · the same entry in another collection · chain M against M, TM-score 1.00
- P84092 · AlphaFold monomer V2.0 prediction for ap-2 complex subunit mu (P84092) · a predicted model of the same protein · chain M against A, TM-score 0.95
- P51577 · AlphaFold monomer V2.0 prediction for P2X purinoceptor 4 (P51577) · a predicted model of the same protein · chain P against A, TM-score 0.36
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 P84092
- Every structure of UniProt P51577
- Elsewhere: RCSB PDB 2BP5 · PDBe 2BP5 · UniProt P84092 · UniProt P51577
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