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Spatial structure of the lentil lipid transfer protein in complex with anionic lysolipid lppg

Analyse Spatial structure of the lentil lipid transfer protein in complex with anionic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5LQV
Type
protein
Length
93 residues
Chains
1
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Non-specific lipid-transfer protein 2
UniProt
A0AT29
Ligands
PGM
Pockets
1 · best druggability 0.78

Structure

solution nmr · 1 distinct chain · 57% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ANon-specific lipid-transfer protein 2protein9357% helix, 0% strandA0AT29

Ligands and binding sites

  • PGM · 1-myristoyl-2-hydroxy-sn-glycero-3-[phospho-rac-(1-glycerol)] · ligand · 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
14560.780.8640PGM

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

  • 5LQV · Spatial structure of the lentil lipid transfer protein in complex with anionic lysolipid… · the same entry in another collection · chain A against A, TM-score 1.00
  • A0AT29 · AlphaFold monomer V2.0 prediction for non-specific lipid-transfer protein 2 (A0AT29) · a predicted model of the same protein · chain A against A, TM-score 0.90

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