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Structural basis of non-specific lipid binding in maize lipid-transfer protein complexes with ricinoleic acid revealed by high-resolution X- ray crystallography

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

PDB
1FK7
Type
protein
Length
93 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Non-specific lipid transfer protein
UniProt
P19656
Ligands
RCL
Pockets
1 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 61% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ANon-specific lipid transfer proteinprotein9361% helix, 0% strandP19656

Ligands and binding sites

  • RCL · Ricinoleic acid · ligand · chains A
  • FMT · Formic acid · additive · chains A

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
12790.750.8733RCL

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

  • 1FK7 · Structural basis of non-specific lipid binding in maize lipid-transfer protein complexes… · the same entry in another collection · chain A against A, TM-score 1.00
  • P19656 · AlphaFold monomer V2.0 prediction for non-specific lipid-transfer protein (P19656) · a predicted model of the same protein · chain A against A, TM-score 0.97

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