3A5O

Crystal Structure of a Dictyostelium P109I Ca2+-Actin in Complex with Human Gelsolin Segment 1

Functional Information from GO Data

Chain	GOid	namespace	contents
C	0000281	biological_process	mitotic cytokinesis
C	0000902	biological_process	cell morphogenesis
C	0001778	biological_process	plasma membrane repair
C	0001891	cellular_component	phagocytic cup
C	0005200	molecular_function	structural constituent of cytoskeleton
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0005811	cellular_component	lipid droplet
C	0005856	cellular_component	cytoskeleton
C	0005884	cellular_component	actin filament
C	0005911	cellular_component	cell-cell junction
C	0005938	cellular_component	cell cortex
C	0006897	biological_process	endocytosis
C	0006909	biological_process	phagocytosis
C	0006935	biological_process	chemotaxis
C	0006972	biological_process	hyperosmotic response
C	0007010	biological_process	cytoskeleton organization
C	0015629	cellular_component	actin cytoskeleton
C	0016192	biological_process	vesicle-mediated transport
C	0016787	molecular_function	hydrolase activity
C	0017022	molecular_function	myosin binding
C	0030027	cellular_component	lamellipodium
C	0030139	cellular_component	endocytic vesicle
C	0030864	cellular_component	cortical actin cytoskeleton
C	0031143	cellular_component	pseudopodium
C	0031252	cellular_component	cell leading edge
C	0032009	cellular_component	early phagosome
C	0032010	cellular_component	phagolysosome
C	0042331	biological_process	phototaxis
C	0045335	cellular_component	phagocytic vesicle
C	0051591	biological_process	response to cAMP
C	0060187	cellular_component	cell pole
C	0061836	cellular_component	intranuclear rod
C	0061851	cellular_component	leading edge of lamellipodium
C	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	HOH1031
S	HOH1117

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

Chain	Residue
S	GLY92
S	ALA94
S	HOH1004
S	HOH1082
C	GLU167
C	HOH1223
S	ASP87

---

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

Chain	Residue
C	ATP376
C	HOH1001
C	HOH1008
C	HOH1050
C	HOH1065
C	HOH1108

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

Chain	Residue
C	GLY13
C	SER14
C	GLY15
C	MET16
C	LYS18
C	GLY156
C	ASP157
C	GLY158
C	VAL159
C	GLY182
C	ARG210
C	LYS213
C	GLU214
C	GLY301
C	GLY302
C	THR303
C	MET305
C	PHE306
C	CA377
C	HOH1009
C	HOH1065
C	HOH1108
C	HOH1134
C	HOH1164
C	HOH1222
C	HOH1294
C	HOH1305

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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
C	TYR53-GLY63

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

Chain	Residue	Details
C	TRP356-GLU364

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

Chain	Residue	Details
C	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
S	ASP44
S	GLU75
S	ASP87
S	GLY92
S	ALA94
S	VAL123
C	TYR53

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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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