3LVR

The crystal structure of ASAP3 in complex with Arf6 in transition state soaked with Calcium

Functional Information from GO Data

Chain	GOid	namespace	contents
E	0001726	cellular_component	ruffle
E	0001889	biological_process	liver development
E	0003924	molecular_function	GTPase activity
E	0003925	molecular_function	G protein activity
E	0005096	molecular_function	GTPase activator activity
E	0005515	molecular_function	protein binding
E	0005525	molecular_function	GTP binding
E	0005737	cellular_component	cytoplasm
E	0005768	cellular_component	endosome
E	0005769	cellular_component	early endosome
E	0005794	cellular_component	Golgi apparatus
E	0005829	cellular_component	cytosol
E	0005886	cellular_component	plasma membrane
E	0005925	cellular_component	focal adhesion
E	0005938	cellular_component	cell cortex
E	0006886	biological_process	intracellular protein transport
E	0007155	biological_process	cell adhesion
E	0007399	biological_process	nervous system development
E	0010975	biological_process	regulation of neuron projection development
E	0010976	biological_process	positive regulation of neuron projection development
E	0015031	biological_process	protein transport
E	0016020	cellular_component	membrane
E	0016192	biological_process	vesicle-mediated transport
E	0016787	molecular_function	hydrolase activity
E	0019003	molecular_function	GDP binding
E	0030139	cellular_component	endocytic vesicle
E	0030154	biological_process	cell differentiation
E	0030496	cellular_component	midbody
E	0030838	biological_process	positive regulation of actin filament polymerization
E	0030866	biological_process	cortical actin cytoskeleton organization
E	0031527	cellular_component	filopodium membrane
E	0031901	cellular_component	early endosome membrane
E	0031996	molecular_function	thioesterase binding
E	0032154	cellular_component	cleavage furrow
E	0032456	biological_process	endocytic recycling
E	0034394	biological_process	protein localization to cell surface
E	0035020	biological_process	regulation of Rac protein signal transduction
E	0035591	molecular_function	signaling adaptor activity
E	0036010	biological_process	protein localization to endosome
E	0042995	cellular_component	cell projection
E	0043547	biological_process	positive regulation of GTPase activity
E	0048261	biological_process	negative regulation of receptor-mediated endocytosis
E	0048488	biological_process	synaptic vesicle endocytosis
E	0050714	biological_process	positive regulation of protein secretion
E	0051301	biological_process	cell division
E	0051489	biological_process	regulation of filopodium assembly
E	0051549	biological_process	positive regulation of keratinocyte migration
E	0055037	cellular_component	recycling endosome
E	0055038	cellular_component	recycling endosome membrane
E	0060998	biological_process	regulation of dendritic spine development
E	0070062	cellular_component	extracellular exosome
E	0072659	biological_process	protein localization to plasma membrane
E	0090162	biological_process	establishment of epithelial cell polarity
E	0090543	cellular_component	Flemming body
E	0097178	biological_process	ruffle assembly
E	0097284	biological_process	hepatocyte apoptotic process
E	0098793	cellular_component	presynapse
E	0098794	cellular_component	postsynapse
E	0098978	cellular_component	glutamatergic synapse
E	0099562	biological_process	maintenance of postsynaptic density structure
E	0120183	biological_process	positive regulation of focal adhesion disassembly
E	1902217	biological_process	erythrocyte apoptotic process
E	1903078	biological_process	positive regulation of protein localization to plasma membrane
E	1903438	biological_process	positive regulation of mitotic cytokinetic process
E	1905345	biological_process	protein localization to cleavage furrow
E	1905606	biological_process	regulation of presynapse assembly
E	1990090	biological_process	cellular response to nerve growth factor stimulus
E	2000009	biological_process	negative regulation of protein localization to cell surface
E	2000171	biological_process	negative regulation of dendrite development

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN E 735

Chain	Residue
E	CYS441
E	CYS444
E	CYS461
E	CYS464
E	ARG527

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site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MG E 736

Chain	Residue
E	HOH220
E	GDP737
E	AF3738
E	LYS26
E	THR27
E	THR44
E	ASP63

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site_id	AC3
Number of Residues	20
Details	BINDING SITE FOR RESIDUE GDP E 737

Chain	Residue
E	ALA23
E	ALA24
E	GLY25
E	LYS26
E	THR27
E	THR28
E	THR41
E	ASN122
E	LYS123
E	ASP125
E	LEU126
E	CYS155
E	ALA156
E	THR157
E	HOH220
E	GLY466
E	ARG469
E	GLU470
E	MG736
E	AF3738

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site_id	AC4
Number of Residues	13
Details	BINDING SITE FOR RESIDUE AF3 E 738

Chain	Residue
E	ASP22
E	ALA23
E	LYS26
E	THR27
E	THR44
E	GLY65
E	GLY66
E	GLN67
E	HOH220
E	HOH230
E	ARG469
E	MG736
E	GDP737

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site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA E 739

Chain	Residue
E	ASP68
E	GLU98
E	HOH232
E	GLN479

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	23
Details	ZN_FING: C4-type => ECO:0000255|PROSITE-ProRule:PRU00288

Chain	Residue	Details
E	CYS441-CYS464

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site_id	SWS_FT_FI2
Number of Residues	5
Details	BINDING: BINDING => ECO:0000269|PubMed:16099990, ECO:0000269|PubMed:19644450, ECO:0000269|PubMed:21170023, ECO:0000269|PubMed:22939626, ECO:0000269|PubMed:23940353

Chain	Residue	Details
E	ALA23
E	THR41
E	ASP63
E	ASN122
E	CYS155

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