Structure of PDB 5dlv Chain B

Receptor sequence
>5dlvB (length=781) Species: 10116 (Rattus norvegicus) [Search protein sequence]
GSCKGRCFELQEVGPPDCRCDNLCKSYSSCCHDFDELCLKTARGWECTKD
RCGEVRNEENACHCSEDCLSRGDCCTNYQVVCKGESHWVDDDCEEIKVPE
CPAGFVRPPLIIFSVDGFRASYMKKGSKVMPNIEKLRSCGTHAPYMRPVY
PTKTFPNLYTLATGLYPESHGIVGNSMYDPVFDASFHLRGREKFNHRWWG
GQPLWITATKQGVRAGTFFWSVSIPHERRILTILQWLSLPDNERPSVYAF
YSEQPDFSGHKYGPFGPEMTNPLREIDKTVGQLMDGLKQLRLHRCVNVIF
VGDHGMEDVTCDRTEFLSNYLTNVDDITLVPGTLGRIRAKSINNSKYDPK
TIIAALTCKKPDQHFKPYMKQHLPKRLHYANNRRIEDIHLLVDRRWHVAR
KPLDVCFFQGDHGFDNKVNSMQTVFVGYGPTFKYRTKVPPFENIELYNVM
CDLLGLKPAPNNGTHGSLNHLLRTNTFRPTMPDEVSRPNYPGIMYLQSEF
DLGCTCDHTKGSTKERHLLYGRPAVLYRTSYDILYHTDFESGYSEIFLMP
LWTSYTISKQAEVSSIPEHLTNCVRPDVRVSPGFSQNCLAYKNDKQMSYG
FLFPPYLSSSPEAKYDAFLVTNMVPMYPAFKRVWAYFQRVLVKKYASERN
GVNVISGPIFDYNYDGLRDTEDEIKQYVEGSSIPVPTHYYSIITSCLDFT
QPADKCDGPLSVSSFILPHRPDNDESCASSEDESKWVEELMKMHTARVRD
IEHLTGLDFYRKTSRSYSEILTLKTYLHTYE
3D structure
PDB5dlv Steroid binding to Autotaxin links bile salts and lysophosphatidic acid signalling.
ChainB
Resolution2.0 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 MAN B E223 S224 N436 E168 S169 N381
BS02 ZN B D311 H315 H474 D256 H260 H412
BS03 ZN B D171 T209 D358 H359 D116 T154 D303 H304
BS04 CA B D739 N741 D743 L745 D747 D661 N663 D665 L667 D669
BS05 5D5 B S81 K248 F249 H251 W254 F274 V277 Y306 S26 K193 F194 H196 W199 F219 V222 Y251 MOAD: ic50=10.4uM
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
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:5dlv, PDBe:5dlv, PDBj:5dlv
PDBsum5dlv
PubMed27075612
UniProtQ64610|ENPP2_RAT Autotaxin (Gene Name=Enpp2)

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