Structure of PDB 2xr9 Chain A

Receptor sequence
>2xr9A (length=783) Species: 10116 (Rattus norvegicus) [Search protein sequence]
GSCKGRCFELQEVGPPDCRCDNLCKSYSSCCHDFDELCLKTARGWECTKD
RCGEVRNEENACHCSEDCLSRGDCCTNYQVVCKGESHWVDDDCEEIKVPE
CPAGFVRPPLIIFSVDGFRASYMKKGSKVMPNIEKLRSCGTHAPYMRPVY
PTKTFPNLYTLATGLYPESHGIVGNSMYDPVFDASFHLRGREKFNHRWWG
GQPLWITATKQGVRAGTFFWSVSIPHERRILTILQWLSLPDNERPSVYAF
YSEQPDFSGHKYGPFGPEMTNPLREIDKTVGQLMDGLKQLRLHRCVNVIF
VGDHGMEDVTCDRTEFLSNYLTNVDDITLVPGTLGRIRAKSIYDPKTIIA
ALTCKKPDQHFKPYMKQHLPKRLHYANNRRIEDIHLLVDRRWHVARKPCF
FQGDHGFDNKVNSMQTVFVGYGPTFKYRTKVPPFENIELYNVMCDLLGLK
PAPNNGTHGSLNHLLRTNTFRPTMPDEVSRPNYPGIMYLQSEFDLGCTCD
KLEELNKRLHTKGSTKERHLLYGRPAVLYRTSYDILYHTDFESGYSEIFL
MPLWTSYTISKQAEVSSIPEHLTNCVRPDVRVSPGFSQNCLAYKNDKQMS
YGFLFPPYLSSSPEAKYDAFLVTNMVPMYPAFKRVWAYFQRVLVKKYASE
RNGVNVISGPIFDYNYDGLRDTEDEIKQYVEGSSIPVPTHYYSIITSCLD
FTQPADKCDGPLSVSSFILPHRPDNDESCNSSEDESKWVEELMKMHTARV
RDIEHLTGLDFYRKTSRSYSEILTLKTYLHTYE
3D structure
PDB2xr9 Structural basis of substrate discrimination and integrin binding by autotaxin.
ChainA
Resolution2.05 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 A D311 H315 H474 D256 H260 H405
BS02 ZN A D171 T209 D358 H359 D116 T154 D303 H304
BS03 CA A D739 N741 D743 L745 D747 D663 N665 D667 L669 D671
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
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Cellular Component
External links
PDB RCSB:2xr9, PDBe:2xr9, PDBj:2xr9
PDBsum2xr9
PubMed21240271
UniProtQ64610|ENPP2_RAT Autotaxin (Gene Name=Enpp2)

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