Structure of PDB 5lqq Chain A

Receptor sequence
>5lqqA (length=775) Species: 10116 (Rattus norvegicus) [Search protein sequence]
GSCKGRCFELQEVGPPDCRCDNLCKSYSSCCHDFDELCLKTARGWECTKD
RCGEVRNEENACHCSEDCLSRGDCCTNYQVVCKGESHWVDDDCEEIKVPE
CPAGFVRPPLIIFSVDGFRASYMKKGSKVMPNIEKLRSCGTHAPYMRPVY
PTKTFPNLYTLATGLYPESHGIVGNSMYDPVFDASFHLRGREKFNHRWWG
GQPLWITATKQGVRAGTFFWSVSIPHERRILTILQWLSLPDNERPSVYAF
YSEQPDFSGHKYGPFGPEMTNPLREIDKTVGQLMDGLKQLRLHRCVNVIF
VGDHGMEDVTCDRTEFLSNYLTNVDDITLVPGTLGRIRAKSINNSKYDPK
TIIAALTCKKPDQHFKPYMKQHLPKRLHYANNRRIEDIHLLVDRRWHVAR
KPLDFQGDHGFDNKVNSMQTVFVGYGPTFKYRTKVPPFENIELYNVMCDL
LGLKPAPNNGTHGSLNHLLRTNTFRPTMPDEVSRPNYPGIMYLQSEFDLG
CTCKGSTKERHLLYGRPAVLYRTSYDILYHTDFESGYSEIFLMPLWTSYT
ISKQAEVSSIPEHLTNCVRPDVRVSPGFSQNCLAYKNDKQMSYGFLFPPY
LSSSPEAKYDAFLVTNMVPMYPAFKRVWAYFQRVLVKKYASERNGVNVIS
GPIFDYNYDGLRDTEDEIKQYVEGSSIPVPTHYYSIITSCLDFTQPADKC
DGPLSVSSFILPHRPDNDESCASSEDESKWVEELMKMHTARVRDIEHLTG
LDFYRKTSRSYSEILTLKTYLHTYE
3D structure
PDB5lqq Structure-Activity Relationships of Small Molecule Autotaxin Inhibitors with a Discrete Binding Mode.
ChainA
Resolution2.4 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 A E223 S224 N436 E168 S169 N381
BS02 ZN A D311 H315 H474 D256 H260 H409
BS03 ZN A D171 T209 D358 H359 D116 T154 D303 H304
BS04 CA A D739 N741 D743 L745 D747 D655 N657 D659 L661 D663
BS05 72P A K248 F249 H251 W254 W260 F274 K193 F194 H196 W199 W205 F219 MOAD: ic50=81nM
PDBbind-CN: -logKd/Ki=7.09,IC50=81nM
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:5lqq, PDBe:5lqq, PDBj:5lqq
PDBsum5lqq
PubMed27982588
UniProtQ64610|ENPP2_RAT Autotaxin (Gene Name=Enpp2)

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