Research workbench
Beta appendage of AP2 complexed with arh peptide
Analyse Beta appendage of AP2 complexed with arh peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2G30
- Type
- protein
- Length
- 252 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ap-2 complex subunit beta-1; 16-mer peptide from low density lipoprotein receptor adapter…
- UniProt
- P63010, Q5SW96
- Pockets
- 1 · best druggability 0.39
Structure
x-ray diffraction · 3 distinct chains · 23% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ap-2 complex subunit beta-1 | protein | 233 | 20% helix, 41% strand | P63010 |
| P | 16-mer peptide from low density lipoprotein receptor adapter protein 1 | protein | 16 | 69% helix, 0% strand | Q5SW96 |
| S | Peptide sequence aaf | protein | 3 | 0% helix, 0% strand | — |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 93 | 0.39 | 0.76 | 22 | empty |
Interfaces
2 interfaces between chains.
- A–P · 694 Ų buried · 9 hydrogen bonds · protein-protein
- A–S · 223 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 2G30 · beta appendage of AP2 complexed with ARH peptide · the same entry in another collection · chain A against A, TM-score 1.00
- P63010 · AlphaFold monomer V2.0 prediction for ap-2 complex subunit beta (P63010) · a predicted model of the same protein · chain A against A, TM-score 0.99
- Q5SW96 · AlphaFold monomer V2.0 prediction for low density lipoprotein receptor adapter protein 1… · a predicted model of the same protein · chain P against A, TM-score 0.67
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 P63010
- Every structure of UniProt Q5SW96
- Elsewhere: RCSB PDB 2G30 · PDBe 2G30 · UniProt P63010 · UniProt Q5SW96
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