Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3ULE

Structure of Bos taurus Arp2/3 complex with bound inhibitor CK-869 and ATP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003779	molecular_function	actin binding
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005856	cellular_component	cytoskeleton
A	0005885	cellular_component	Arp2/3 protein complex
A	0010592	biological_process	positive regulation of lamellipodium assembly
A	0030030	biological_process	cell projection organization
A	0034314	biological_process	Arp2/3 complex-mediated actin nucleation
A	0035861	cellular_component	site of double-strand break
A	0042995	cellular_component	cell projection
A	0045944	biological_process	positive regulation of transcription by RNA polymerase II
A	0051015	molecular_function	actin filament binding
A	0060271	biological_process	cilium assembly
B	0000166	molecular_function	nucleotide binding
B	0003779	molecular_function	actin binding
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0005856	cellular_component	cytoskeleton
B	0005885	cellular_component	Arp2/3 protein complex
B	0005938	cellular_component	cell cortex
B	0010592	biological_process	positive regulation of lamellipodium assembly
B	0034314	biological_process	Arp2/3 complex-mediated actin nucleation
B	0035861	cellular_component	site of double-strand break
B	0042995	cellular_component	cell projection
B	0045944	biological_process	positive regulation of transcription by RNA polymerase II
B	0051015	molecular_function	actin filament binding
B	1905168	biological_process	positive regulation of double-strand break repair via homologous recombination
B	2001032	biological_process	regulation of double-strand break repair via nonhomologous end joining
C	0003779	molecular_function	actin binding
C	0005634	cellular_component	nucleus
C	0005829	cellular_component	cytosol
C	0005856	cellular_component	cytoskeleton
C	0005885	cellular_component	Arp2/3 protein complex
C	0015629	cellular_component	actin cytoskeleton
C	0034314	biological_process	Arp2/3 complex-mediated actin nucleation
C	0051015	molecular_function	actin filament binding
D	0003779	molecular_function	actin binding
D	0005200	molecular_function	structural constituent of cytoskeleton
D	0005634	cellular_component	nucleus
D	0005654	cellular_component	nucleoplasm
D	0005768	cellular_component	endosome
D	0005829	cellular_component	cytosol
D	0005856	cellular_component	cytoskeleton
D	0005885	cellular_component	Arp2/3 protein complex
D	0005886	cellular_component	plasma membrane
D	0005925	cellular_component	focal adhesion
D	0010592	biological_process	positive regulation of lamellipodium assembly
D	0015629	cellular_component	actin cytoskeleton
D	0030027	cellular_component	lamellipodium
D	0030041	biological_process	actin filament polymerization
D	0030672	cellular_component	synaptic vesicle membrane
D	0030838	biological_process	positive regulation of actin filament polymerization
D	0031252	cellular_component	cell leading edge
D	0034314	biological_process	Arp2/3 complex-mediated actin nucleation
D	0035861	cellular_component	site of double-strand break
D	0036195	cellular_component	muscle cell projection membrane
D	0042995	cellular_component	cell projection
D	0043005	cellular_component	neuron projection
D	0045202	cellular_component	synapse
D	0051015	molecular_function	actin filament binding
D	0098793	cellular_component	presynapse
D	0098794	cellular_component	postsynapse
D	0098978	cellular_component	glutamatergic synapse
D	1900026	biological_process	positive regulation of substrate adhesion-dependent cell spreading
E	0003779	molecular_function	actin binding
E	0005515	molecular_function	protein binding
E	0005634	cellular_component	nucleus
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0005856	cellular_component	cytoskeleton
E	0005885	cellular_component	Arp2/3 protein complex
E	0030833	biological_process	regulation of actin filament polymerization
E	0034314	biological_process	Arp2/3 complex-mediated actin nucleation
E	0035861	cellular_component	site of double-strand break
E	0042995	cellular_component	cell projection
E	0051015	molecular_function	actin filament binding
F	0003779	molecular_function	actin binding
F	0005634	cellular_component	nucleus
F	0005829	cellular_component	cytosol
F	0005856	cellular_component	cytoskeleton
F	0005885	cellular_component	Arp2/3 protein complex
F	0015629	cellular_component	actin cytoskeleton
F	0030041	biological_process	actin filament polymerization
F	0034314	biological_process	Arp2/3 complex-mediated actin nucleation
F	0035861	cellular_component	site of double-strand break
F	0042995	cellular_component	cell projection
F	0051015	molecular_function	actin filament binding
G	0003779	molecular_function	actin binding
G	0005634	cellular_component	nucleus
G	0005829	cellular_component	cytosol
G	0005856	cellular_component	cytoskeleton
G	0005885	cellular_component	Arp2/3 protein complex
G	0015629	cellular_component	actin cytoskeleton
G	0016477	biological_process	cell migration
G	0030674	molecular_function	protein-macromolecule adaptor activity
G	0030833	biological_process	regulation of actin filament polymerization
G	0030863	cellular_component	cortical cytoskeleton
G	0034314	biological_process	Arp2/3 complex-mediated actin nucleation
G	0035861	cellular_component	site of double-strand break
G	0042995	cellular_component	cell projection

Functional Information from PDB Data

site_id	AC1
Number of Residues	21
Details	BINDING SITE FOR RESIDUE ATP A 1001

Chain	Residue
A	GLY13
A	GLY197
A	LYS225
A	LYS228
A	GLU229
A	GLY324
A	MET327
A	PHE328
A	ARG374
A	CA1003
A	HOH1107
A	THR14
A	HOH1115
A	HOH1120
A	GLY15
A	TYR16
A	LYS18
A	ASP169
A	GLY171
A	ASP172
A	GLY173

site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE C69 A 1002

Chain	Residue
A	PRO77
A	GLU84
A	TRP86
A	MET89
A	THR113
A	PRO115
A	ASN118
A	ASN122
A	THR126
A	ILE129

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CA A 1003

Chain	Residue
A	GLN144
A	ATP1001
A	HOH1112

site_id	AC4
Number of Residues	19
Details	BINDING SITE FOR RESIDUE ATP B 401

Chain	Residue
B	GLY14
B	THR15
B	GLY16
B	PHE17
B	GLY160
B	ASP161
B	GLY162
B	GLY186
B	ARG214
B	LYS217
B	GLU218
B	GLY306
B	SER307
B	MET309
B	TYR310
B	CA402
B	HOH501
B	HOH506
B	HOH522

site_id	AC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CA B 402

Chain	Residue
B	ATP401

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
B	LEU108-ARG120
A	LEU111-ARG123

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"UniProtKB","id":"P61158","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P61158","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	11
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15505213","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17499050","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P61160","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	39
Details	Repeat: {"description":"WD 1"}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	39
Details	Repeat: {"description":"WD 2"}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	41
Details	Repeat: {"description":"WD 3"}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	39
Details	Repeat: {"description":"WD 4"}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	38
Details	Repeat: {"description":"WD 5"}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	43
Details	Repeat: {"description":"WD 6"}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"O15144","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"O15145","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"O15145","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"UniProtKB","id":"O15145","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	1
Details	Modified residue: {"description":"N-acetylthreonine","evidences":[{"source":"UniProtKB","id":"P59998","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)