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1OIP

The Molecular Basis of Vitamin E Retention: Structure of Human Alpha-Tocopherol Transfer Protein

Functional Information from GO Data
ChainGOidnamespacecontents
A0001890biological_processplacenta development
A0001892biological_processembryonic placenta development
A0005515molecular_functionprotein binding
A0005546molecular_functionphosphatidylinositol-4,5-bisphosphate binding
A0005737cellular_componentcytoplasm
A0005770cellular_componentlate endosome
A0005829cellular_componentcytosol
A0006629biological_processlipid metabolic process
A0008289molecular_functionlipid binding
A0008431molecular_functionvitamin E binding
A0009636biological_processresponse to toxic substance
A0042360biological_processvitamin E metabolic process
A0043325molecular_functionphosphatidylinositol-3,4-bisphosphate binding
A0051180biological_processvitamin transport
A0090212biological_processnegative regulation of establishment of blood-brain barrier
A0120009biological_processintermembrane lipid transfer
A0120013molecular_functionlipid transfer activity
A1900223biological_processpositive regulation of amyloid-beta clearance
A1902936molecular_functionphosphatidylinositol bisphosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A1276
ChainResidue
ALYS190
AARG192
ALYS217
AARG221
AHOH2124

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A1277
ChainResidue
AHIS223
AHIS225
ASER232
AHIS236

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE VIV A1278
ChainResidue
ASER136
ASER140
AILE154
APHE158
AVAL182
ALEU183
APHE187
AVAL191
AHOH2050
AHOH2125

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q8BWP5
ChainResidueDetails
AASP185
APHE187
ALYS190
ASER208
ALYS217
AARG221

236963

PDB entries from 2025-06-04

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