MolNFT v1 · #48373 · protein
MU2 adaptin subunit (AP50) of AP2 adaptor (second domain), complexed with gabaa receptor-GAMMA2 subunit-derived internalization peptide deeygyecl
2PR9 · Ap-2 complex subunit mu-1: “MU2 adaptin subunit (AP50) of AP2 adaptor (second domain), complexed with gabaa receptor-GAMMA2…”. X-ray diffraction, 3 pockets (best druggability 0.39). MolNFT v1 #48373 on GenesisL1: 3D structure…
- PDB
- 2PR9
- Type
- protein
- Length
- 264 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ap-2 complex subunit mu-1; GABA(A) receptor subunit gamma-2 peptide
- UniProt
- P84092, P18508
- Pockets
- 3 · best druggability 0.39
Structure
x-ray diffraction · 2 distinct chains · 2% helix, 56% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ap-2 complex subunit mu-1 | protein | 254 | 2% helix, 58% strand | P84092 |
| P | GABA(A) receptor subunit gamma-2 peptide | protein | 10 | 0% helix, 20% strand | P18508 |
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 | 96 | 0.39 | 0.76 | 18 | empty |
| 2 | 96 | 0.34 | 0.73 | 25 | empty |
| 3 | 53 | 0.28 | 0.74 | 16 | empty |
Interfaces
1 interface between chains.
- A–P · 582 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 2PR9 · Mu2 adaptin subunit (AP50) of AP2 adaptor (second domain), complexed with GABAA… · the same entry in another collection · chain A against A, 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 A against A, TM-score 0.95
- P18508 · AlphaFold monomer V2.0 prediction for gamma-aminobutyric acid receptor subunit gamma-2… · a predicted model of the same protein · chain P against A, TM-score 0.35
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 P18508
- Elsewhere: RCSB PDB 2PR9 · PDBe 2PR9 · UniProt P84092 · UniProt P18508
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