Structure of PDB 3lvq Chain E
Receptor sequence
>3lvqE (length=420) Species:
9606
(Homo sapiens) [
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DLTKLLIAEVKSRPGNSQCCDCGAADPTWLSTNLGVLTCIQCSGVHRELG
VRFSRMQSLTLDLLGPSELLLALNMGNTSFNEVMEAQLPSHGGPKPSAES
DMGTRRDYIMAKYVEHRFARRCTEPQRLWTAICNRDLLSVLEAFANGQDF
GQPLPGPDAQAPEELVLHLAVKVANQASLPLVDFIIQNGGHLDAKAADGN
TALHYAALYNQPDCLKLLLKGRALVGTVNEAGETALDIARKKHHKECEEL
LEQAQANKEMRILMLGLDAAGKTTILYKLKLGQSVTTIPTVGFNVETVTY
KNVKFNVWDVGGQDKIRPLWRHYYTGTQGLIFVVDCADRDRIDEARQELH
RIINDREMRDAIILIFANKQDLPDAMKPHEIQEKLGLTRIRDRNWYVQPS
CATSGDGLYEGLTWLTSNYK
3D structure
PDB
3lvq
The structure of an Arf-ArfGAP complex reveals a Ca2+ regulatory mechanism
Chain
E
Resolution
3.38 Å
3D
structure
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Enzymatic activity
Enzyme Commision number
?
3.6.5.2
: small monomeric GTPase.
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
E
C441 C444 C461 C464
C19 C22 C39 C42
BS02
MG
E
T27 T44
T273 T290
BS03
GDP
E
R469 E470 A23 A24 G25 K26 T27 T28 T41 N122 K123 D125 L126 C155 A156 T157
R47 E48 A269 A270 G271 K272 T273 T274 T287 N368 K369 D371 L372 C401 A402 T403
BS04
AF3
E
R469 D22 A23 K26 T44 G66 Q67
R47 D268 A269 K272 T290 G312 Q313
Gene Ontology
Molecular Function
GO:0003924
GTPase activity
GO:0003925
G protein activity
GO:0005096
GTPase activator activity
GO:0005515
protein binding
GO:0005525
GTP binding
GO:0016787
hydrolase activity
GO:0019003
GDP binding
GO:0031996
thioesterase binding
GO:0035591
signaling adaptor activity
Biological Process
GO:0001889
liver development
GO:0006886
intracellular protein transport
GO:0007155
cell adhesion
GO:0007399
nervous system development
GO:0010975
regulation of neuron projection development
GO:0010976
positive regulation of neuron projection development
GO:0015031
protein transport
GO:0016192
vesicle-mediated transport
GO:0030154
cell differentiation
GO:0030838
positive regulation of actin filament polymerization
GO:0030866
cortical actin cytoskeleton organization
GO:0032456
endocytic recycling
GO:0034394
protein localization to cell surface
GO:0035020
regulation of Rac protein signal transduction
GO:0036010
protein localization to endosome
GO:0043547
positive regulation of GTPase activity
GO:0048261
negative regulation of receptor-mediated endocytosis
GO:0048488
synaptic vesicle endocytosis
GO:0050714
positive regulation of protein secretion
GO:0051301
cell division
GO:0051489
regulation of filopodium assembly
GO:0051549
positive regulation of keratinocyte migration
GO:0060998
regulation of dendritic spine development
GO:0072659
protein localization to plasma membrane
GO:0090162
establishment of epithelial cell polarity
GO:0097178
ruffle assembly
GO:0097284
hepatocyte apoptotic process
GO:0099562
maintenance of postsynaptic density structure
GO:0120183
positive regulation of focal adhesion disassembly
GO:1902217
erythrocyte apoptotic process
GO:1903078
positive regulation of protein localization to plasma membrane
GO:1903438
positive regulation of mitotic cytokinetic process
GO:1905345
protein localization to cleavage furrow
GO:1905606
regulation of presynapse assembly
GO:1990090
cellular response to nerve growth factor stimulus
GO:2000009
negative regulation of protein localization to cell surface
GO:2000171
negative regulation of dendrite development
Cellular Component
GO:0001726
ruffle
GO:0005737
cytoplasm
GO:0005768
endosome
GO:0005769
early endosome
GO:0005794
Golgi apparatus
GO:0005829
cytosol
GO:0005886
plasma membrane
GO:0005925
focal adhesion
GO:0005938
cell cortex
GO:0016020
membrane
GO:0030139
endocytic vesicle
GO:0030496
midbody
GO:0031527
filopodium membrane
GO:0031901
early endosome membrane
GO:0032154
cleavage furrow
GO:0042995
cell projection
GO:0055037
recycling endosome
GO:0055038
recycling endosome membrane
GO:0070062
extracellular exosome
GO:0090543
Flemming body
GO:0098793
presynapse
GO:0098794
postsynapse
GO:0098978
glutamatergic synapse
View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB
RCSB:3lvq
,
PDBe:3lvq
,
PDBj:3lvq
PDBsum
3lvq
PubMed
20510928
UniProt
P62330
|ARF6_HUMAN ADP-ribosylation factor 6 (Gene Name=ARF6);
Q8TDY4
|ASAP3_HUMAN Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 3 (Gene Name=ASAP3)
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