Research workbench
AlphaFold monomer V2.0 prediction for phosphatidylinositol transfer protein alpha isoform (P53810)
Analyse AlphaFold monomer V2.0 prediction for phosphatidylinositol transfer protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P53810
- Type
- protein
- Length
- 271 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x738c1929c69B751bD0Be0B962D9bac20B631aAc6
- Molecule
- Phosphatidylinositol transfer protein alpha isoform
- UniProt
- P53810
- Pockets
- 2 · best druggability 0.89
Structure
1 distinct chain · 34% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphatidylinositol transfer protein alpha isoform | protein | 271 | 34% helix, 27% strand | P53810 |
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 | 769 | 0.89 | 0.92 | 74 | empty |
| 2 | 64 | 0.32 | 0.76 | 19 | empty |
Compared structures
- 1KCM · Crystal Structure of Mouse PITP Alpha Void of Bound Phospholipid at 2.0 Angstroms… · an experimental structure of the same protein · chain A against A, TM-score 0.81
- 1KCM · Crystal structure of mouse pitp alpha void of bound phospholipid at 2.0 ångströms… · an experimental structure of the same protein · chain A against A, TM-score 0.81
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 P53810
- Elsewhere: UniProt P53810 · AlphaFold DB P53810
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