Research workbench
Seipin forms a flexible cage at lipid droplet formation sites
Analyse Seipin forms a flexible cage at lipid droplet formation sites in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7RSL
- Type
- protein
- Length
- 2,350 residues
- Chains
- 10
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Seipin
- UniProt
- Q06058
- Pockets
- 20 · best druggability 0.61
Structure
electron microscopy · 1 distinct chain · 30% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, G, H, E, F, I, J, C, D | Seipin | protein | 235 | 30% helix, 36% strand | Q06058 |
Pockets
20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 206 | 0.61 | 0.82 | 34 | empty |
| 2 | 231 | 0.60 | 0.80 | 35 | empty |
| 3 | 246 | 0.59 | 0.79 | 35 | empty |
| 4 | 193 | 0.58 | 0.81 | 34 | empty |
| 5 | 257 | 0.58 | 0.79 | 36 | empty |
Interfaces
10 interfaces between chains.
- C–D · 1704 Ų buried · 12 hydrogen bonds · protein-protein
- G–H · 1698 Ų buried · 12 hydrogen bonds · protein-protein
- I–J · 1695 Ų buried · 12 hydrogen bonds · protein-protein
- E–F · 1692 Ų buried · 12 hydrogen bonds · protein-protein
- A–B · 1691 Ų buried · 12 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 Q06058
- Elsewhere: RCSB PDB 7RSL · PDBe 7RSL · UniProt Q06058
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