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Crystal structure of the ptb domain of human APPL1
Analyse Crystal structure of the ptb domain of human APPL1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ELA
- Type
- protein
- Length
- 272 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Adapter protein containing pH domain, ptb domain and leucine zipper motif 1
- UniProt
- Q9UKG1
- Pockets
- 2 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 33% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Adapter protein containing pH domain, ptb domain and leucine zipper motif 1 | protein | 131 | 30% helix, 44% strand | Q9UKG1 |
| B | Adapter protein containing pH domain, ptb domain and leucine zipper motif 1 | protein | 141 | 36% helix, 43% strand | Q9UKG1 |
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 629 | 0.80 | 0.85 | 59 | empty |
| 2 | 52 | 0.69 | 0.97 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 1008 Ų buried · 9 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 Q9UKG1
- Elsewhere: RCSB PDB 2ELA · PDBe 2ELA · UniProt Q9UKG1
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