1R5L

Crystal Structure of Human Alpha-Tocopherol Transfer Protein Bound to its Ligand

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001890	biological_process	placenta development
A	0001892	biological_process	embryonic placenta development
A	0005515	molecular_function	protein binding
A	0005546	molecular_function	phosphatidylinositol-4,5-bisphosphate binding
A	0005737	cellular_component	cytoplasm
A	0005770	cellular_component	late endosome
A	0005829	cellular_component	cytosol
A	0006629	biological_process	lipid metabolic process
A	0008289	molecular_function	lipid binding
A	0008431	molecular_function	vitamin E binding
A	0009636	biological_process	response to toxic substance
A	0042360	biological_process	vitamin E metabolic process
A	0043325	molecular_function	phosphatidylinositol-3,4-bisphosphate binding
A	0051180	biological_process	vitamin transport
A	0090212	biological_process	negative regulation of establishment of blood-brain barrier
A	0120009	biological_process	intermembrane lipid transfer
A	0120013	molecular_function	lipid transfer activity
A	1900223	biological_process	positive regulation of amyloid-beta clearance
A	1902936	molecular_function	phosphatidylinositol bisphosphate binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE VIV A 301

Chain	Residue
A	SER136
A	HOH302
A	HOH402
A	SER140
A	ILE154
A	PHE158
A	VAL182
A	LEU183
A	PHE187
A	VAL191
A	ILE210

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	BINDING: BINDING => ECO:0000250|UniProtKB:Q8BWP5

Chain	Residue	Details
A	ASP185
A	PHE187
A	LYS190
A	SER208
A	LYS217
A	ARG221

---