Structure of PDB 5l0k Chain B

Receptor sequence
>5l0kB (length=777) Species: 10116 (Rattus norvegicus) [Search protein sequence]
TATSGSCKGRCFELQEVGPPDCRCDNLCKSYSSCCHDFDELCLKTARGWE
CTKDRCGEVRNEENACHCSEDCLSRGDCCTNYQVVCKGESHWVDDDCEEI
KVPECPAGFVRPPLIIFSVDGFRASYMKKVMPNIEKLRSCGTHAPYMRPV
YPTKTFPNLYTLATGLYPESHGIVGNSMYDPVFDASFHLRGREKFNHRWW
GGQPLWITATKQGVRAGTFFWSVSIPHERRILTILQWLSLPDNERPSVYA
FYSEQPDFSGHKYGPFGPEMTNPLREIDKTVGQLMDGLKQLRLHRCVNVI
FVGDHGMEDVTCDRTEFLSNYLTNVDDITLVPGTLGRIRAKSIANSKYDP
KTIIAALTCKKPDQHFKPYMKQHLPKRLHYANNRRIEDIHLLVDRRWHVA
RKPLDVCFFQGDHGFDNKVNSMQTVFVGYGPTFKYRTKVPPFENIELYNV
MCDLLGLKPAPNNGTHGSLNHLLRTNTFRPTMPDEVSRPNYPGIMYLQSE
FDLGCTCDTEERHLLYGRPAVLYRTSYDILYHTDFESGYSEIFLMPLWTS
YTISKQAEVSSIPEHLTNCVRPDVRVSPGFSQNCLAYKNDKQMSYGFLFP
PYLSSSPEAKYDAFLVTNMVPMYPAFKRVWAYFQRVLVKKYASERNGVNV
ISGPIFDYNYDGLRDTEDEIKQYVEGSSIPVPTHYYSIITSCLDFTQPAD
KCDGPLSVSSFILPHRPDNDESCASSEDESKWVEELMKMHTARVRDIEHL
TGLDFYRKTSRSYSEILTLKTYLHTYE
3D structure
PDB5l0k Novel Autotaxin Inhibitors for the Treatment of Osteoarthritis Pain: Lead Optimization via Structure-Based Drug Design.
ChainB
Resolution2.73 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.1.4.39: alkylglycerophosphoethanolamine phosphodiesterase.
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 ZN B D311 H315 H474 D257 H261 H413
BS02 ZN B D171 T209 D358 H359 D120 T155 D304 H305
BS03 CA B D739 N741 D743 L745 D747 D657 N659 D661 L663 D665
BS04 6ZO B D171 T209 L213 Y214 F273 F274 W275 Y306 D311 D120 T155 L159 Y160 F219 F220 W221 Y252 D257 BindingDB: IC50=307nM
Gene Ontology
Molecular Function
GO:0003676 nucleic acid binding
GO:0004528 phosphodiesterase I activity
GO:0004622 lysophospholipase activity
GO:0004630 phospholipase D activity
GO:0005044 scavenger receptor activity
GO:0005509 calcium ion binding
GO:0008270 zinc ion binding
GO:0016787 hydrolase activity
GO:0016788 hydrolase activity, acting on ester bonds
GO:0030247 polysaccharide binding
GO:0046872 metal ion binding
GO:0047391 alkylglycerophosphoethanolamine phosphodiesterase activity
Biological Process
GO:0001953 negative regulation of cell-matrix adhesion
GO:0006644 phospholipid metabolic process
GO:0006935 chemotaxis
GO:0006955 immune response
GO:0008284 positive regulation of cell population proliferation
GO:0009395 phospholipid catabolic process
GO:0010634 positive regulation of epithelial cell migration
GO:0016042 lipid catabolic process
GO:0016192 vesicle-mediated transport
GO:0030149 sphingolipid catabolic process
GO:0030334 regulation of cell migration
GO:0034638 phosphatidylcholine catabolic process
GO:0044849 estrous cycle
GO:0048714 positive regulation of oligodendrocyte differentiation
GO:0050731 positive regulation of peptidyl-tyrosine phosphorylation
GO:0051894 positive regulation of focal adhesion assembly
GO:0060326 cell chemotaxis
GO:0071276 cellular response to cadmium ion
GO:0071392 cellular response to estradiol stimulus
GO:1900026 positive regulation of substrate adhesion-dependent cell spreading
GO:1903165 response to polycyclic arene
GO:2000394 positive regulation of lamellipodium morphogenesis
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space

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Molecular Function
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Biological Process
View graph for
Cellular Component
External links
PDB RCSB:5l0k, PDBe:5l0k, PDBj:5l0k
PDBsum5l0k
PubMed27660691
UniProtQ64610|ENPP2_RAT Autotaxin (Gene Name=Enpp2)

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