Research workbench
Lipid-protein interactions in lipovitellin
Analyse Lipid-protein interactions in lipovitellin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1LSH
- Type
- protein
- Length
- 1,129 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lipovitellin (lv-1N, lv-1C); Lipovitellin (lv-2)
- UniProt
- Q91062
- Ligands
- UPL, PLD
- Pockets
- 14 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 28% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lipovitellin (lv-1N, lv-1C) | protein | 955 | 31% helix, 37% strand | Q91062 |
| B | Lipovitellin (lv-2) | protein | 174 | 14% helix, 50% strand | Q91062 |
Ligands and binding sites
- UPL · Unknown branched fragment of phospholipid · ligand · 43 copies · chains A, B
- PLD · di-heneicosanoyl phosphatidyl choline · ligand · 7 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 791 | 0.78 | 0.81 | 87 | PLD |
| 2 | 85 | 0.76 | 0.98 | 38 | empty |
| 3 | 210 | 0.72 | 0.87 | 35 | UPL |
| 4 | 192 | 0.67 | 0.86 | 40 | empty |
| 5 | 177 | 0.62 | 0.84 | 32 | empty |
Interfaces
1 interface between chains.
- A–B · 1056 Ų buried · 18 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide, 1 modified (disulfide, cyclization).
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 Q91062
- Elsewhere: RCSB PDB 1LSH · PDBe 1LSH · UniProt Q91062
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