Structure of PDB 5ohi Chain A

Receptor sequence
>5ohiA (length=778) Species: 10090 (Mus musculus) [Search protein sequence]
WTNTSGSCKGRCFELQEVGPPDCRCDNLCKSYSSCCHDFDELCLKTARGW
ECTKDRCGEVRNEENACHCSEDCLSRGDCCTNYQVVCKGESHWVDDDCEE
IRVPECPAGFVRPPLIIFSVDGFRASYMKKGSKVMPNIEKLRSCGTHAPY
MRPVYPTKTFPNLYTLATGLYPESHGIVGNSMYDPVFDATFHLRGREKFN
HRWWGGQPLWITATKQGVRAGTFFWSVSIPHERRILTILQWLSLPDNERP
SVYAFYSEQPDFSGHKYGPFGPEMTNPLREIDKTVGQLMDGLKQLKLHRC
VNVIFVGDHGMEDVTCDRTEFLSNYLTNVDDITLVPGTLGRIRPKIPNNL
KYDPKAIIANLTCKKPDQHFKPYMKQHLPKRLHYANNRRIEDLHLLVERR
WHVARKPLDCFFQGDHGFDNKVNSMQTVFVGYGPTFKYRTKVPPFENIEL
YNVMCDLLGLKPAPNNGTHGSLNHLLRTNTFRPTLPEEVSRPNYPGIMYL
QSDFDLGCTCEERHLLYGRPAVLYRTSYDILYHTDFESGYSEIFLMPLWT
SYTISKQAEVSSIPEHLTNCVRPDVRVSPGFSQNCLAYKNDKQMSYGFLF
PPYLSSSPEAKYDAFLVTNMVPMYPAFKRVWTYFQRVLVKKYASERNGVN
VISGPIFDYNYNGLRDIEDEIKQYVEGSSIPVPTHYYSIITSCLDFTQPA
DKCDGPLSVSSFILPHRPDNDESCNSSEDESKWVEELMKMHTARVRDIEH
LTGLDFYRKTSRSYSEILTLKTYLHTYE
3D structure
PDB5ohi Discovery of BI-2545: A Novel Autotaxin Inhibitor That Significantly Reduces LPA Levels in Vivo.
ChainA
Resolution1.66 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 S224 G255 S174 G205
BS02 MAN A E223 S224 N436 E173 S174 N386
BS03 ZN A D311 H315 H474 D261 H265 H416
BS04 ZN A D171 T209 D358 H359 D121 T159 D308 H309
BS05 CA A D735 N737 N739 L741 D743 D658 N660 N662 L664 D666
BS06 9V8 A D171 T209 F210 L213 Y214 L243 W260 F273 F274 W275 Y306 D311 D121 T159 F160 L163 Y164 L193 W210 F223 F224 W225 Y256 D261 PDBbind-CN: -logKd/Ki=8.47,IC50=3.4nM
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:5ohi, PDBe:5ohi, PDBj:5ohi
PDBsum5ohi
PubMed29259743
UniProtQ9R1E6|ENPP2_MOUSE Autotaxin (Gene Name=Enpp2)

[Back to BioLiP]