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Crystal structure of non-specific lipid transfer protein reveals non- canonical lipid binding: possible relevance in modulating allergenicity

Analyse Crystal structure of non-specific lipid transfer protein reveals non- canonical… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5TVI
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
Ligands
MYR, O8N
Pockets
1 · best druggability 0.57

Structure

x-ray diffraction · 2 distinct chains · 65% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
VNon specific lipid transfer proteinprotein9066% helix, 0% strand—
WNon specific lipid transfer proteinprotein9265% helix, 0% strand—

Ligands and binding sites

  • MYR · Myristic acid · ligand · chains V
  • O8N · octacosan-1-ol · ligand · chains W
  • GOL · Glycerol · additive · chains V

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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1500.570.9017empty

Interfaces

1 interface between chains.

  • V–W · 740 Ų buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

  • 5TVI · Crystal structure of non-specific lipid transfer protein reveals non-canonical lipid… · the same entry in another collection · chain V against V, TM-score 1.00

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