Research workbench
Structure of the pleckstrin homology domain from DAPP1/PHISH in complex with inositol 1,3,4,5- tetrakisphosphate
Analyse Structure of the pleckstrin homology domain from DAPP1/PHISH in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1FAO
- Type
- protein
- Length
- 100 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dual adaptor of phosphotyrosine and 3- phosphoinositides
- UniProt
- Q9UN19
- Ligands
- 4IP
Structure
x-ray diffraction · 1 distinct chain · 19% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dual adaptor of phosphotyrosine and 3- phosphoinositides | protein | 100 | 19% helix, 43% strand | Q9UN19 |
Ligands and binding sites
- 4IP · Inositol-(1,3,4,5)-tetrakisphosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 1FAO · Structure of the pleckstrin homology domain from DAPP1/PHISH in complex with inositol… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9UN19 · AlphaFold monomer V2.0 prediction for dual adapter for phosphotyrosine and… · a predicted model of the same protein · chain A against A, TM-score 0.97
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 Q9UN19
- Elsewhere: RCSB PDB 1FAO · PDBe 1FAO · UniProt Q9UN19
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.