Research workbench
Structure of pitp-alpha complexed to phosphatidylinositol
Analyse Structure of pitp-alpha complexed to phosphatidylinositol in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1UW5
- Type
- protein
- Length
- 1,075 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphatidylinositol transfer protein alpha isoform
- UniProt
- Q00169
- Ligands
- PIE
- Pockets
- 10 · best druggability 0.88
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Phosphatidylinositol transfer protein alpha isoform | protein | 269 | 36% helix, 28% strand | Q00169 |
| D | Phosphatidylinositol transfer protein alpha isoform | protein | 268 | 36% helix, 28% strand | Q00169 |
Ligands and binding sites
- PIE · 1,2-diacyl-sn-glycero-3-phosphoinositol · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 736 | 0.88 | 0.92 | 75 | PIE |
| 2 | 817 | 0.88 | 0.90 | 76 | PIE |
| 3 | 806 | 0.87 | 0.90 | 78 | PIE |
| 4 | 766 | 0.87 | 0.90 | 76 | PIE |
| 5 | 676 | 0.72 | 0.79 | 65 | empty |
Interfaces
3 interfaces between chains.
- A–B · 486 Ų buried · 7 hydrogen bonds · protein-protein
- B–C · 281 Ų buried · 2 hydrogen bonds · protein-protein
- A–D · 63 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 32 modified (engineered).
Compared structures
- 1UW5 · Structure of PITP-alpha complexed to phosphatidylinositol · the same entry in another collection · chain A against A, TM-score 1.00
- Q00169 · AlphaFold monomer V2.0 prediction for phosphatidylinositol transfer protein alpha isoform… · a predicted model of the same protein · chain D against A, TM-score 0.99
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 Q00169
- Elsewhere: RCSB PDB 1UW5 · PDBe 1UW5 · UniProt Q00169
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