MolNFT v1 · #152888 · protein
Structural insight into probable lipid transfer mechanism of non- specific lipid transfer protein via intermediate structures in solanum melongena
6IWO · Non-specific lipid-transfer protein: “Structural insight into probable lipid transfer mechanism of non- specific lipid transfer protein via…”. X-ray diffraction, 2 ligands (MYR, SO4), 1 pocket (best druggability 0.69). MolNFT v1…
- PDB
- 6IWO
- Type
- protein
- Length
- 182 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Non-specific lipid-transfer protein
- UniProt
- A0A247D6Y2
- Ligands
- MYR, SO4
- Pockets
- 1 · best druggability 0.69
Structure
x-ray diffraction · 2 distinct chains · 67% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Non-specific lipid-transfer protein | protein | 92 | 66% helix, 0% strand | A0A247D6Y2 |
| B | Non-specific lipid-transfer protein | protein | 90 | 68% helix, 0% strand | A0A247D6Y2 |
Ligands and binding sites
- MYR · Myristic acid · ligand · chains A, B
- SO4 · Sulfate ion · ion · 2 copies · chains B
- GOL · Glycerol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 52 | 0.69 | 0.97 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 757 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 disulfide (disulfide).
Compared structures
- 6IWO · Structural insight into probable lipid transfer mechanism of non-specific lipid transfer… · the same entry in another collection · chain A against A, TM-score 1.00
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 A0A247D6Y2
- Elsewhere: RCSB PDB 6IWO · PDBe 6IWO · UniProt A0A247D6Y2
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