Research workbench
Structure of human phosphatidylcholine transfer protein in complex with palmitoyl-linoleoyl phosphatidylcholine (seleno-met protein)
Analyse 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
- 1LN3
- Type
- protein
- Length
- 406 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphatidylcholine transfer protein
- UniProt
- Q9UKL6
- Ligands
- CPL
- Pockets
- 4 · best druggability 0.86
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Phosphatidylcholine transfer protein | protein | 203 | 27% helix, 38% strand | Q9UKL6 |
Ligands and binding sites
- CPL · 1-palmitoyl-2-linoleoyl-sn-glycero-3-phosphocholine · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 898 | 0.86 | 0.88 | 57 | CPL |
| 2 | 862 | 0.86 | 0.87 | 54 | CPL |
| 3 | 99 | 0.40 | 0.76 | 15 | empty |
| 4 | 111 | 0.38 | 0.75 | 14 | empty |
Modifications
Observed in the structure: 12 modified (engineered).
Compared structures
- 1LN3 · 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
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 Q9UKL6
- Elsewhere: RCSB PDB 1LN3 · PDBe 1LN3 · UniProt Q9UKL6
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