Research workbench
B2-appendage from AP2 in complex with EPS15 peptide
Analyse B2-appendage from AP2 in complex with EPS15 peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2IV9
- Type
- protein
- Length
- 478 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ap-2 complex subunit beta-2; Epidermal growth factor receptor substrate 15 isoform B
- UniProt
- P63010, Q5JC29
- Ligands
- SO4
- Pockets
- 5 · best druggability 0.56
Structure
x-ray diffraction · 3 distinct chains · 19% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ap-2 complex subunit beta-2 | protein | 236 | 18% helix, 41% strand | P63010 |
| B | Ap-2 complex subunit beta-2 | protein | 233 | 19% helix, 41% strand | P63010 |
| P | Epidermal growth factor receptor substrate 15 isoform B | protein | 9 | 44% helix, 0% strand | Q5JC29 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 216 | 0.56 | 0.79 | 29 | empty |
| 2 | 165 | 0.50 | 0.78 | 25 | empty |
| 3 | 105 | 0.41 | 0.76 | 20 | empty |
| 4 | 93 | 0.37 | 0.75 | 17 | empty |
| 5 | 84 | 0.37 | 0.76 | 16 | empty |
Interfaces
3 interfaces between chains.
- A–B · 631 Ų buried · 3 hydrogen bonds · protein-protein
- A–P · 414 Ų buried · 4 hydrogen bonds · protein-protein
- B–P · 361 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
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 Q5JC29
- Elsewhere: RCSB PDB 2IV9 · PDBe 2IV9 · UniProt P63010 · UniProt Q5JC29
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