Structure of PDB 2euk Chain A

Receptor sequence
>2eukA (length=204) Species: 9606 (Homo sapiens) [Search protein sequence]
LAEHLLKPLPADKQIETGPFLEAVSHLPPFFDCLGSPVFTPIKADISGNI
TKIKAVYDTNPAKFRTLQNILEVEKEMYGAEWPKVGATLALMWLKRGLRF
IQVFLQSICDGERDENHPNLIRVNATKAYEMALKKYHGWIVQKIFQAALY
AAPYKSDFLKALSQNVTEEECLEKIRLFLVNYTATIDVIYEMYTQMNAEL
NYKV
3D structure
PDB2euk The liganding of glycolipid transfer protein is controlled by glycolipid acyl structure.
ChainA
Resolution1.85 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 GAL A D48 N52 K55 W96 Y207 D45 N49 K52 W93 Y202 PDBbind-CN: -logKd/Ki=6.60,Kd=0.25uM
BS02 SPH A D48 W96 D45 W93 PDBbind-CN: -logKd/Ki=6.60,Kd=0.25uM
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0008289 lipid binding
GO:0017089 glycolipid transfer activity
GO:0042802 identical protein binding
GO:0051861 glycolipid binding
GO:0120013 lipid transfer activity
GO:1902387 ceramide 1-phosphate binding
GO:1902388 ceramide 1-phosphate transfer activity
Biological Process
GO:0006869 lipid transport
GO:0035627 ceramide transport
GO:0035902 response to immobilization stress
GO:0046836 glycolipid transport
GO:0120009 intermembrane lipid transfer
GO:1902389 ceramide 1-phosphate transport
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Cellular Component
External links
PDB RCSB:2euk, PDBe:2euk, PDBj:2euk
PDBsum2euk
PubMed17105344
UniProtQ9NZD2|GLTP_HUMAN Glycolipid transfer protein (Gene Name=GLTP)

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