Structure of PDB 5m0m Chain A
Receptor sequence
>5m0mA (length=774) Species:
10116
(Rattus norvegicus) [
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SGSCKGRCFELQEVGPPDCRCDNLCKSYSSCCHDFDELCLKTARGWECTK
DRCGEVRNEENACHCSEDCLSRGDCCTNYQVVCKGESHWVDDDCEEIKVP
ECPAGFVRPPLIIFSVDGFRASYMKKGSKVMPNIEKLRSCGTHAPYMRPV
YPTKTFPNLYTLATGLYPESHGIVGNSMYDPVFDASFHLRGREKFNHRWW
GGQPLWITATKQGVRAGTFFWSVSIPHERRILTILQWLSLPDNERPSVYA
FYSEQPDFSGHKYGPFGPEMTNPLREIDKTVGQLMDGLKQLRLHRCVNVI
FVGDHGMEDVTCDRTEFLSNYLTNVDDITLVPGTLGRIRAKSINNSKYDP
KTIIAALTCKKPDQHFKPYMKQHLPKRLHYANNRRIEDIHLLVDRRWHVA
RKPLFQGDHGFDNKVNSMQTVFVGYGPTFKYRTKVPPFENIELYNVMCDL
LGLKPAPNNGTHGSLNHLLRTNTFRPTMPDEVSRPNYPGIMYLQSEFDLG
CTCDSTKERHLLYGRPAVLYRTSYDILYHTDFESGYSEIFLMPLWTSYTI
SKQAEVSSIPEHLTNCVRPDVRVSPGFSQNCLAYKNDKQMSYGFLFPPYL
SSSPEAKYDAFLVTNMVPMYPAFKRVWAYFQRVLVKKYASERNGVNVISG
PIFDYNYDGLRDTEDEIKQYVEGSSIPVPTHYYSIITSCLDFTQPADKCD
GPLSVSSFILPHRPDNDESCASSEDESKWVEELMKMHTARVRDIEHLTGL
DFYRKTSRSYSEILTLKTYLHTYE
3D structure
PDB
5m0m
Rational Design of Autotaxin Inhibitors by Structural Evolution of Endogenous Modulators.
Chain
A
Resolution
2.1 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
E169 S170 N382
BS02
MAN
A
Q257 K265
Q203 K211
BS03
ZN
A
D311 H315 H474
D257 H261 H409
BS04
ZN
A
D171 T209 D358 H359
D117 T155 D304 H305
BS05
CA
A
D739 N741 D743 L745 D747
D654 N656 D658 L660 D662
BS06
7CF
A
Y82 S169 F210 L213 K248 F249 W254 W260 F273 F274 W275 Y306
Y28 S115 F156 L159 K194 F195 W200 W206 F219 F220 W221 Y252
PDBbind-CN
: -logKd/Ki=8.22,Ki=6nM
BS07
NKP
A
P70 S81 R246 K248 F249
P16 S27 R192 K194 F195
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:5m0m
,
PDBe:5m0m
,
PDBj:5m0m
PDBsum
5m0m
PubMed
28165241
UniProt
Q64610
|ENPP2_RAT Autotaxin (Gene Name=Enpp2)
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