1NMD

Crystal Structure of D. Discoideum Actin-Gelsolin Segment 1 Complex Crystallized In Presence Of Lithium ATP

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	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	HOH414
G	HOH422

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 404

Chain	Residue
A	ASP311
A	HOH546
A	HOH642
A	GLY308
A	ILE309
A	ALA310

---

site_id	AC3
Number of Residues	26
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	GLY182
A	ARG183
A	ARG210
A	LYS213
A	GLU214
A	GLY301
A	GLY302
A	THR303
A	MET305
A	LYS336
A	HOH408
A	HOH416
A	HOH423
A	HOH424
A	HOH438
A	HOH439
A	HOH468
A	HOH478
A	HOH562

---

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO2 A 403

Chain	Residue
A	ARG62
A	ARG62
A	THR202
A	THR203
A	ALA204
A	HOH500
A	HOH500
A	HOH626

---

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

---

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

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"7498488","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	82
Details	Repeat: {"description":"Gelsolin-like 1","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	Region: {"description":"Actin-actin interfilament contact point"}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	7
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19666512","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3FFK","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	7
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine; by SRC; in vitro","evidences":[{"source":"PubMed","id":"10210201","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---