Structure of PDB 6ob0 Chain A

Receptor sequence
>6ob0A (length=442) Species: 9606 (Homo sapiens) [Search protein sequence]
QRRDFIDIESKFALRTPEDTAEDTCHLIPGVAESVATCHFNHSSKTFMVI
HGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLSRAQEHYPVSAGYTK
LVGQDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGIAGSLTNKKVNRI
TGLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGH
VDIYPNGGTFQPGCNIGEAIRVIAERGLGDVDQLVKCSHERSIHLFIDSL
LNEENPSKAYRCSSKEAFEKGLCLSCRKNRCNNLGYEINKVRAKRSSKMY
LKTRSQMPYKVFHYQVKIHFSGTESETHTNQAFEISLYGTVAESENIPFT
LPEVSTNKTYSFLIYTEVDIGELLMLKLKWKSDSYFSWSDWWSSPGFAIQ
KIRVKAGETQKKVIFCSREKVSHLQKGKAPAVFVKCHDKSLN
3D structure
PDB6ob0 Structure of lipoprotein lipase in complex with GPIHBP1.
ChainA
Resolution2.81 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 H239
Enzyme Commision number 3.1.1.32: phospholipase A1.
3.1.1.34: lipoprotein lipase.
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 M3D A W82 V84 L263 W53 V55 L234 PDBbind-CN: -logKd/Ki=4.96,Kd~11uM
BS02 M3D A W82 Y121 S159 K265 H268 W53 Y92 S130 K236 H239 PDBbind-CN: -logKd/Ki=4.96,Kd~11uM
BS03 CA A A194 R197 S199 D202 A165 R168 S170 D173
BS04 M3D A F415 W417 F386 W388 PDBbind-CN: -logKd/Ki=4.96,Kd~11uM
BS05 M3D A W420 W421 W391 W392 PDBbind-CN: -logKd/Ki=4.96,Kd~11uM
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:6ob0, PDBe:6ob0, PDBj:6ob0
PDBsum6ob0
PubMed31072929
UniProtP06858|LIPL_HUMAN Lipoprotein lipase (Gene Name=LPL)

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