1C0G

CRYSTAL STRUCTURE OF 1:1 COMPLEX BETWEEN GELSOLIN SEGMENT 1 AND A DICTYOSTELIUM/TETRAHYMENA CHIMERA ACTIN (MUTANT 228: Q228K/T229A/A230Y/E360H)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000281	biological_process	mitotic cytokinesis
A	0000902	biological_process	cell morphogenesis
A	0001778	biological_process	plasma membrane repair
A	0001891	cellular_component	phagocytic cup
A	0005200	molecular_function	structural constituent of cytoskeleton
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005811	cellular_component	lipid droplet
A	0005856	cellular_component	cytoskeleton
A	0005884	cellular_component	actin filament
A	0005911	cellular_component	cell-cell junction
A	0005938	cellular_component	cell cortex
A	0006897	biological_process	endocytosis
A	0006909	biological_process	phagocytosis
A	0006935	biological_process	chemotaxis
A	0006972	biological_process	hyperosmotic response
A	0007010	biological_process	cytoskeleton organization
A	0015629	cellular_component	actin cytoskeleton
A	0016192	biological_process	vesicle-mediated transport
A	0016787	molecular_function	hydrolase activity
A	0017022	molecular_function	myosin binding
A	0030027	cellular_component	lamellipodium
A	0030139	cellular_component	endocytic vesicle
A	0030864	cellular_component	cortical actin cytoskeleton
A	0031143	cellular_component	pseudopodium
A	0031252	cellular_component	cell leading edge
A	0032009	cellular_component	early phagosome
A	0032010	cellular_component	phagolysosome
A	0042221	biological_process	response to chemical
A	0042331	biological_process	phototaxis
A	0045335	cellular_component	phagocytic vesicle
A	0051591	biological_process	response to cAMP
A	0060187	cellular_component	cell pole
A	0061836	cellular_component	intranuclear rod
A	0061851	cellular_component	leading edge of lamellipodium
A	0070685	cellular_component	macropinocytic cup
S	0051015	molecular_function	actin filament binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA S 128

Chain	Residue
S	GLY43
S	ASP44
S	GLU75
S	VAL123
S	HOH139
S	HOH179

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site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CA S 129

Chain	Residue
S	ALA94
S	HOH130
S	HOH162
S	HOH192
A	GLU167
S	ASP87
S	GLY92

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site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 377

Chain	Residue
A	ATP376
A	HOH378
A	HOH382
A	HOH405
A	HOH413
A	HOH439

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site_id	AC4
Number of Residues	27
Details	BINDING SITE FOR RESIDUE ATP A 376

Chain	Residue
A	GLY13
A	SER14
A	GLY15
A	MET16
A	LYS18
A	GLY156
A	ASP157
A	GLY158
A	VAL159
A	GLY182
A	ARG210
A	LYS213
A	GLU214
A	GLY301
A	GLY302
A	THR303
A	MET305
A	PHE306
A	CA377
A	HOH383
A	HOH413
A	HOH439
A	HOH450
A	HOH467
A	HOH507
A	HOH550
A	HOH559

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Functional Information from PROSITE/UniProt

site_id	PS00406
Number of Residues	11
Details	ACTINS_1 Actins signature 1. YVGDEAQs.KRG

Chain	Residue	Details
A	TYR53-GLY63

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site_id	PS00432
Number of Residues	9
Details	ACTINS_2 Actins signature 2. WISKhEYDE

Chain	Residue	Details
A	TRP356-GLU364

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site_id	PS01132
Number of Residues	13
Details	ACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR

Chain	Residue	Details
A	LEU104-ARG116

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0000269|PubMed:7498488

Chain	Residue	Details
A	VAL54
S	ASP44
S	GLU75
S	ASP87
S	GLY92
S	ALA94
S	VAL123

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site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
S	LYS113

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by SRC; in vitro => ECO:0000269|PubMed:10210201

Chain	Residue	Details
S	TYR37

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