Structure of PDB 6oau Chain B Binding Site BS01

Receptor Information
>6oau Chain B (length=422) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
QRRDFIDIESKFALRTPEDTAEDTCHLIPGVAESVATCHFNHSSKTFMVI
HGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLSRAQEHYPVSAGYTK
LVGQDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGIAGSLTNKKVNRI
TGLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGH
VDIYPNGGTFQPGCNIGVDQLVKCSHERSIHLFIDSLLNEENPSKAYRCS
SKEAFEKGLCLSCRKNRCNNLGYEINKVRAKRSSKMYLKTRSQMPYKVFH
YQVKIHFSGTESETHTNQAFEISLYGTVAESENIPFTLPEVSTNKTYSFL
IYTEVDIGELLMLKLKWKSDWWSSPGFAIQKIRVKAGETQKKVIFCSREK
VSHLQKGKAPAVFVKCHDKSLN
Ligand information
Ligand IDCA
InChIInChI=1S/Ca/q+2
InChIKeyBHPQYMZQTOCNFJ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Ca++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Ca+2]
FormulaCa
NameCALCIUM ION
ChEMBL
DrugBankDB14577
ZINC
PDB chain6oau Chain B Residue 503 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB6oau Structure of lipoprotein lipase in complex with GPIHBP1.
Resolution2.48 Å
Binding residue
(original residue number in PDB)		A194 R197 S199 D202
Binding residue
(residue number reindexed from 1)		A165 R168 S170 D173
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) W82 S159 L160 D183 H268
Catalytic site (residue number reindexed from 1) W53 S130 L131 D154 H226
Enzyme Commision number 3.1.1.32: phospholipase A1.
3.1.1.34: lipoprotein lipase.
Gene Ontology
Molecular Function
GO:0004465 lipoprotein lipase activity
GO:0004620 phospholipase activity
GO:0004806 triacylglycerol lipase activity
GO:0005102 signaling receptor binding
GO:0005509 calcium ion binding
GO:0005515 protein binding
GO:0008201 heparin binding
GO:0008970 phospholipase A1 activity
GO:0016298 lipase activity
GO:0016787 hydrolase activity
GO:0034185 apolipoprotein binding
GO:0042803 protein homodimerization activity
GO:0043395 heparan sulfate proteoglycan binding
GO:0043495 protein-membrane adaptor activity
GO:0046872 metal ion binding
GO:0052689 carboxylic ester hydrolase activity
GO:0052739 phosphatidylserine 1-acylhydrolase activity
GO:0071813 lipoprotein particle binding
Biological Process
GO:0006629 lipid metabolic process
GO:0006631 fatty acid metabolic process
GO:0006633 fatty acid biosynthetic process
GO:0006641 triglyceride metabolic process
GO:0006644 phospholipid metabolic process
GO:0009617 response to bacterium
GO:0009749 response to glucose
GO:0010744 positive regulation of macrophage derived foam cell differentiation
GO:0010884 positive regulation of lipid storage
GO:0010886 positive regulation of cholesterol storage
GO:0010890 positive regulation of sequestering of triglyceride
GO:0016042 lipid catabolic process
GO:0019433 triglyceride catabolic process
GO:0031670 cellular response to nutrient
GO:0032722 positive regulation of chemokine production
GO:0032731 positive regulation of interleukin-1 beta production
GO:0032755 positive regulation of interleukin-6 production
GO:0032760 positive regulation of tumor necrosis factor production
GO:0034371 chylomicron remodeling
GO:0034372 very-low-density lipoprotein particle remodeling
GO:0034375 high-density lipoprotein particle remodeling
GO:0042632 cholesterol homeostasis
GO:0045600 positive regulation of fat cell differentiation
GO:0050729 positive regulation of inflammatory response
GO:0055096 low-density lipoprotein particle mediated signaling
GO:0070328 triglyceride homeostasis
GO:0071398 cellular response to fatty acid
GO:1904179 positive regulation of adipose tissue development
GO:2000343 positive regulation of chemokine (C-X-C motif) ligand 2 production
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0005886 plasma membrane
GO:0009986 cell surface
GO:0034361 very-low-density lipoprotein particle
GO:0042627 chylomicron
GO:1902494 catalytic complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6oau, PDBe:6oau, PDBj:6oau
PDBsum6oau
PubMed31072929
UniProtP06858|LIPL_HUMAN Lipoprotein lipase (Gene Name=LPL)

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