Research workbench
AlphaFold monomer V2.0 prediction for PHOSPHATIDYLGLYCEROL/PHOSPHATIDYLINOSITOL transfer protein (Q12408)
Analyse AlphaFold monomer V2.0 prediction for PHOSPHATIDYLGLYCEROL/PHOSPHATIDYLINOSITOL… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q12408
- Type
- protein
- Length
- 173 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7782F4817b37743d738e9aF842bf74bd50f2015E
- Molecule
- PHOSPHATIDYLGLYCEROL/PHOSPHATIDYLINOSITOL transfer protein
- UniProt
- Q12408
- Pockets
- 1 · best druggability 0.80
Structure
1 distinct chain · 13% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | PHOSPHATIDYLGLYCEROL/PHOSPHATIDYLINOSITOL transfer protein | protein | 173 | 13% helix, 45% strand | Q12408 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 819 | 0.80 | 0.82 | 55 | empty |
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 6R4N · Crystal structure of S. cerevisia Niemann-Pick type C protein NPC2 with ergosterol bound · an experimental structure of the same protein · chain A against I, TM-score 0.81
- 6R4N · Crystal structure of S. cerevisia niemann-pick type C protein NPC2 with ergosterol bound · an experimental structure of the same protein · chain A against A, TM-score 0.81
- 6R4M · Crystal structure of S. cerevisia niemann-pick type C protein NPC2 · an experimental structure of the same protein · chain A against A, TM-score 0.80
- 6R4M · Crystal structure of S. cerevisia Niemann-Pick type C protein NPC2 · an experimental structure of the same protein · chain A against A, TM-score 0.80
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 Q12408
- Elsewhere: UniProt Q12408 · AlphaFold DB Q12408
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