Structure of PDB 1oiz Chain A

Receptor sequence
>1oizA (length=265) Species: 9606 (Homo sapiens) [Search protein sequence]
SAGPQLNALPDHSPLLQPGLAALRRRAREAGVPLAPLPLTDSFLLRFLRA
RDFDLDLAWRLLKNYYKWRAECPEISADLHPRSIIGLLKAGYHGVLRSRD
PTGSKVLIYRIAHWDPKVFTAYDVFRVSLITSELIVQEVETQRNGIKAIF
DLEGWQFSHAFQITPSVAKKIAAVLTDSFPLKVRGIHLINEPVIFHAVFS
MIKPFLTEKIKERIHMHGNNYKQSLLQHFPDILPLEYGGEEFSMEDICQE
WTNFIMKSEDYLSSI
3D structure
PDB1oiz The Molecular Basis of Vitamin E Retention: Structure of Human Alpha-Tocopherol Transfer Protein
ChainA
Resolution1.88 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 TRT A W163 F165 I202 F203 V206 I222 M224 W155 F157 I194 F195 V198 I214 M216
BS02 TRT A L115 S136 S140 I154 V182 L183 L107 S128 S132 I146 V174 L175
BS03 TRT A W163 A168 I171 W155 A160 I163
BS04 TRT A M209 I210 M201 I202
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0005546 phosphatidylinositol-4,5-bisphosphate binding
GO:0008289 lipid binding
GO:0008431 vitamin E binding
GO:0043325 phosphatidylinositol-3,4-bisphosphate binding
GO:0120013 lipid transfer activity
GO:1902936 phosphatidylinositol bisphosphate binding
Biological Process
GO:0001890 placenta development
GO:0001892 embryonic placenta development
GO:0006629 lipid metabolic process
GO:0009636 response to toxic substance
GO:0042360 vitamin E metabolic process
GO:0051180 vitamin transport
GO:0090212 negative regulation of establishment of blood-brain barrier
GO:0120009 intermembrane lipid transfer
GO:1900223 positive regulation of amyloid-beta clearance
Cellular Component
GO:0005737 cytoplasm
GO:0005770 late endosome
GO:0005829 cytosol

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:1oiz, PDBe:1oiz, PDBj:1oiz
PDBsum1oiz
PubMed12899840
UniProtP49638|TTPA_HUMAN Alpha-tocopherol transfer protein (Gene Name=TTPA)

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