Structure of PDB 3nkq Chain A

Receptor sequence
>3nkqA (length=782) Species: 10090 (Mus musculus) [Search protein sequence]
WTNTSGSCKGRCFELQEVGPPDCRCDNLCKSYSSCCHDFDELCLKTARGW
ECTKDRCGEVRNEENACHCSEDCLSRGDCCTNYQVVCKGESHWVDDDCEE
IRVPECPAGFVRPPLIIFSVDGFRASYMKKGSKVMPNIEKLRSCGTHAPY
MRPVYPTKTFPNLYTLATGLYPESHGIVGNSMYDPVFDATFHLRGREKFN
HRWWGGQPLWITATKQGVRAGTFFWSVSIPHERRILTILQWLSLPDNERP
SVYAFYSEQPDFSGHKYGPFGPEMTNPLREIDKTVGQLMDGLKQLKLHRC
VNVIFVGDHGMEDVTCDRTEFLSNYLTNVDDITLVPGTLGRIRPKIPNNL
KYDPKAIIANLTCKKPDQHFKPYMKQHLPKRLHYANNRRIEDLHLLVERR
WHVARKPLCFFQGDHGFDNKVNSMQTVFVGYGPTFKYRTKVPPFENIELY
NVMCDLLGLKPAPNNGTHGSLNHLLRTNTFRPTLPEEVSRPNYPGIMYLQ
SDFDLGCTCDDGSTEERHLLYGRPAVLYRTSYDILYHTDFESGYSEIFLM
PLWTSYTISKQAEVSSIPEHLTNCVRPDVRVSPGFSQNCLAYKNDKQMSY
GFLFPPYLSSSPEAKYDAFLVTNMVPMYPAFKRVWTYFQRVLVKKYASER
NGVNVISGPIFDYNYNGLRDIEDEIKQYVEGSSIPVPTHYYSIITSCLDF
TQPADKCDGPLSVSSFILPHRPDNDESCNSSEDESKWVEELMKMHTARVR
DIEHLTGLDFYRKTSRSYSEILTLKTYLHTYE
3D structure
PDB3nkq Crystal structure of autotaxin and insight into GPCR activation by lipid mediators
ChainA
Resolution1.7 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 E173 S174 N386
BS02 ZN A D171 T209 D358 H359 D121 T159 D308 H309
BS03 ZN A D311 H315 H474 D261 H265 H415
BS04 CA A D735 N737 N739 L741 D743 D662 N664 N666 L668 D670
BS05 NKQ A T209 F210 L213 N230 Y306 D311 H474 T159 F160 L163 N180 Y256 D261 H415
BS06 NKQ A H251 W254 H201 W204
Gene Ontology
Molecular Function
GO:0003676 nucleic acid binding
GO:0004528 phosphodiesterase I activity
GO:0004551 dinucleotide phosphatase 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:0006644 phospholipid metabolic process
GO:0006935 chemotaxis
GO:0006955 immune response
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:0050731 positive regulation of peptidyl-tyrosine phosphorylation
GO:2000394 positive regulation of lamellipodium morphogenesis
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0005886 plasma membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3nkq, PDBe:3nkq, PDBj:3nkq
PDBsum3nkq
PubMed21240269
UniProtQ9R1E6|ENPP2_MOUSE Autotaxin (Gene Name=Enpp2)

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