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Phenylalanine zipper mediates aps dimerization
Analyse Phenylalanine zipper mediates aps dimerization in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1Q2H
- Type
- protein
- Length
- 188 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Adaptor protein with pleckstrin homology and src homology 2 domains
- UniProt
- O14492
- Pockets
- 2 · best druggability 0.57
Structure
x-ray diffraction · 3 distinct chains · 84% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Adaptor protein with pleckstrin homology and src homology 2 domains | protein | 63 | 87% helix, 0% strand | O14492 |
| B | Adaptor protein with pleckstrin homology and src homology 2 domains | protein | 62 | 84% helix, 0% strand | O14492 |
| C | Adaptor protein with pleckstrin homology and src homology 2 domains | protein | 63 | 79% helix, 0% strand | O14492 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 394 | 0.57 | 0.74 | 43 | empty |
| 2 | 66 | 0.29 | 0.73 | 11 | empty |
Interfaces
3 interfaces between chains.
- A–B · 2031 Ų buried · 5 hydrogen bonds · protein-protein
- B–C · 182 Ų buried · 6 hydrogen bonds · protein-protein
- A–C · 133 Ų buried · 0 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 O14492
- Elsewhere: RCSB PDB 1Q2H · PDBe 1Q2H · UniProt O14492
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