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Crystal structure of human phosphatidylcholine transfer protein in complex with dilinoleoylphosphatidylcholine

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

PDB
1LN1
Type
protein
Length
203 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Phosphatidylcholine transfer protein
UniProt
Q9UKL6
Ligands
DLP
Pockets
2 · best druggability 0.87

Structure

x-ray diffraction · 1 distinct chain · 25% helix, 41% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APhosphatidylcholine transfer proteinprotein20325% helix, 41% strandQ9UKL6

Ligands and binding sites

  • DLP · 1,2-dilinoleoyl-sn-glycero-3-phosphocholine · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18390.870.8854DLP
2940.370.7515empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 1LN1 · Crystal Structure of Human Phosphatidylcholine Transfer Protein in Complex with… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9UKL6 · AlphaFold monomer V2.0 prediction for phosphatidylcholine transfer protein (Q9UKL6) · a predicted model of the same protein · chain A against A, TM-score 0.98

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