1NM1

Crystal Structure of D. Dicsoideum Actin Complexed With Gelsolin Segment 1 and Mg ATP at 1.8 A Resolution

Replaces:  1DGA

Functional Information from GO Data

Chain	GOid	namespace	contents
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	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
G	0051015	molecular_function	actin filament binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA G 402

Chain	Residue
G	GLY41
G	ASP42
G	GLU73
G	VAL121
G	HOH413
G	HOH414

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site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 403

Chain	Residue
A	HOH418
A	HOH445
A	ATP401
A	HOH411
A	HOH417

---

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 A 405

Chain	Residue
A	GLY308
A	ILE309
A	ALA310
A	ASP311
A	HOH481
A	HOH621
G	LYS13

---

site_id	AC4
Number of Residues	30
Details	BINDING SITE FOR RESIDUE ATP A 401

Chain	Residue
A	GLY13
A	SER14
A	GLY15
A	MET16
A	LYS18
A	GLY156
A	ASP157
A	GLY158
A	GLY182
A	ARG183
A	ARG210
A	LYS213
A	GLU214
A	GLY301
A	GLY302
A	THR303
A	MET305
A	PHE306
A	LYS336
A	MG403
A	HOH409
A	HOH417
A	HOH426
A	HOH432
A	HOH444
A	HOH445
A	HOH457
A	HOH493
A	HOH561
A	HOH580

---

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO2 A 404

Chain	Residue
A	ARG62
A	ARG62
A	THR202
A	THR203
A	ALA204

---

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. WISKeEYDE

Chain	Residue	Details
A	TRP356-GLU364

---

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	7
Details	BINDING: BINDING => ECO:0000269|PubMed:19666512, ECO:0007744|PDB:3FFK

Chain	Residue	Details
G	GLY41
G	ASP42
G	GLU73
G	ASP85
G	GLY90
G	ALA92
G	VAL121

---

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

Chain	Residue	Details
G	LYS111

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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
G	TYR35

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