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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7T5Q

Cryo-EM Structure of a Transition State of Arp2/3 Complex Activation

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003779molecular_functionactin binding
A0005200molecular_functionstructural constituent of cytoskeleton
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0005885cellular_componentArp2/3 protein complex
A0010592biological_processpositive regulation of lamellipodium assembly
A0030030biological_processcell projection organization
A0034314biological_processArp2/3 complex-mediated actin nucleation
A0035861cellular_componentsite of double-strand break
A0042995cellular_componentcell projection
A0045944biological_processpositive regulation of transcription by RNA polymerase II
A0051015molecular_functionactin filament binding
A0060271biological_processcilium assembly
B0000166molecular_functionnucleotide binding
B0003779molecular_functionactin binding
B0005200molecular_functionstructural constituent of cytoskeleton
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005856cellular_componentcytoskeleton
B0005885cellular_componentArp2/3 protein complex
B0005938cellular_componentcell cortex
B0010592biological_processpositive regulation of lamellipodium assembly
B0034314biological_processArp2/3 complex-mediated actin nucleation
B0035861cellular_componentsite of double-strand break
B0042995cellular_componentcell projection
B0045944biological_processpositive regulation of transcription by RNA polymerase II
B0051015molecular_functionactin filament binding
B1905168biological_processpositive regulation of double-strand break repair via homologous recombination
B2001032biological_processregulation of double-strand break repair via nonhomologous end joining
C0003779molecular_functionactin binding
C0005634cellular_componentnucleus
C0005856cellular_componentcytoskeleton
C0005885cellular_componentArp2/3 protein complex
C0015629cellular_componentactin cytoskeleton
C0034314biological_processArp2/3 complex-mediated actin nucleation
C0035861cellular_componentsite of double-strand break
C0036195cellular_componentmuscle cell projection membrane
C0045202cellular_componentsynapse
C0051015molecular_functionactin filament binding
C0098978cellular_componentglutamatergic synapse
D0003779molecular_functionactin binding
D0005200molecular_functionstructural constituent of cytoskeleton
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005768cellular_componentendosome
D0005829cellular_componentcytosol
D0005856cellular_componentcytoskeleton
D0005885cellular_componentArp2/3 protein complex
D0005886cellular_componentplasma membrane
D0005925cellular_componentfocal adhesion
D0010592biological_processpositive regulation of lamellipodium assembly
D0015629cellular_componentactin cytoskeleton
D0030027cellular_componentlamellipodium
D0030041biological_processactin filament polymerization
D0030672cellular_componentsynaptic vesicle membrane
D0031252cellular_componentcell leading edge
D0034314biological_processArp2/3 complex-mediated actin nucleation
D0035861cellular_componentsite of double-strand break
D0036195cellular_componentmuscle cell projection membrane
D0042995cellular_componentcell projection
D0043005cellular_componentneuron projection
D0045202cellular_componentsynapse
D0051015molecular_functionactin filament binding
D0098793cellular_componentpresynapse
D0098794cellular_componentpostsynapse
D0098978cellular_componentglutamatergic synapse
E0003779molecular_functionactin binding
E0005515molecular_functionprotein binding
E0005634cellular_componentnucleus
E0005737cellular_componentcytoplasm
E0005829cellular_componentcytosol
E0005856cellular_componentcytoskeleton
E0005885cellular_componentArp2/3 protein complex
E0030833biological_processregulation of actin filament polymerization
E0034314biological_processArp2/3 complex-mediated actin nucleation
E0035861cellular_componentsite of double-strand break
E0042995cellular_componentcell projection
E0051015molecular_functionactin filament binding
F0003779molecular_functionactin binding
F0005634cellular_componentnucleus
F0005829cellular_componentcytosol
F0005856cellular_componentcytoskeleton
F0005885cellular_componentArp2/3 protein complex
F0015629cellular_componentactin cytoskeleton
F0030041biological_processactin filament polymerization
F0034314biological_processArp2/3 complex-mediated actin nucleation
F0035861cellular_componentsite of double-strand break
F0042995cellular_componentcell projection
F0051015molecular_functionactin filament binding
G0003779molecular_functionactin binding
G0005634cellular_componentnucleus
G0005829cellular_componentcytosol
G0005856cellular_componentcytoskeleton
G0005885cellular_componentArp2/3 protein complex
G0015629cellular_componentactin cytoskeleton
G0016477biological_processcell migration
G0030674molecular_functionprotein-macromolecule adaptor activity
G0030833biological_processregulation of actin filament polymerization
G0030863cellular_componentcortical cytoskeleton
G0034314biological_processArp2/3 complex-mediated actin nucleation
G0035861cellular_componentsite of double-strand break
G0042995cellular_componentcell projection
H0000166molecular_functionnucleotide binding
H0000287molecular_functionmagnesium ion binding
H0001725cellular_componentstress fiber
H0003785molecular_functionactin monomer binding
H0005509molecular_functioncalcium ion binding
H0005515molecular_functionprotein binding
H0005523molecular_functiontropomyosin binding
H0005524molecular_functionATP binding
H0005737cellular_componentcytoplasm
H0005856cellular_componentcytoskeleton
H0005865cellular_componentstriated muscle thin filament
H0005884cellular_componentactin filament
H0010628biological_processpositive regulation of gene expression
H0016787molecular_functionhydrolase activity
H0019904molecular_functionprotein domain specific binding
H0030027cellular_componentlamellipodium
H0030041biological_processactin filament polymerization
H0030175cellular_componentfilopodium
H0030240biological_processskeletal muscle thin filament assembly
H0031013molecular_functiontroponin I binding
H0031432molecular_functiontitin binding
H0031941cellular_componentfilamentous actin
H0032036molecular_functionmyosin heavy chain binding
H0032432cellular_componentactin filament bundle
H0042802molecular_functionidentical protein binding
H0044297cellular_componentcell body
H0048306molecular_functioncalcium-dependent protein binding
H0048741biological_processskeletal muscle fiber development
H0051017biological_processactin filament bundle assembly
H0090131biological_processmesenchyme migration
H0098723cellular_componentskeletal muscle myofibril
H0140660molecular_functioncytoskeletal motor activator activity
I0003779molecular_functionactin binding
I0005515molecular_functionprotein binding
I0005576cellular_componentextracellular region
I0005829cellular_componentcytosol
I0005856cellular_componentcytoskeleton
I0007015biological_processactin filament organization
I0008290cellular_componentF-actin capping protein complex
I0015629cellular_componentactin cytoskeleton
I0030036biological_processactin cytoskeleton organization
I0030863cellular_componentcortical cytoskeleton
I0034329biological_processcell junction assembly
I0045296molecular_functioncadherin binding
I0051015molecular_functionactin filament binding
I0051016biological_processbarbed-end actin filament capping
I0051693biological_processactin filament capping
I0065003biological_processprotein-containing complex assembly
I0070062cellular_componentextracellular exosome
I0071203cellular_componentWASH complex
J0003779molecular_functionactin binding
J0005515molecular_functionprotein binding
J0005737cellular_componentcytoplasm
J0005829cellular_componentcytosol
J0005856cellular_componentcytoskeleton
J0005903cellular_componentbrush border
J0007015biological_processactin filament organization
J0008290cellular_componentF-actin capping protein complex
J0014069cellular_componentpostsynaptic density
J0015629cellular_componentactin cytoskeleton
J0016020cellular_componentmembrane
J0030017cellular_componentsarcomere
J0030027cellular_componentlamellipodium
J0030036biological_processactin cytoskeleton organization
J0030863cellular_componentcortical cytoskeleton
J0045296molecular_functioncadherin binding
J0051016biological_processbarbed-end actin filament capping
J0051693biological_processactin filament capping
J0070062cellular_componentextracellular exosome
J0071203cellular_componentWASH complex
J0098685cellular_componentSchaffer collateral - CA1 synapse
J0098686cellular_componenthippocampal mossy fiber to CA3 synapse
J0120212cellular_componentsperm head-tail coupling apparatus
Functional Information from PROSITE/UniProt
site_idPS00231
Number of Residues6
DetailsF_ACTIN_CAPPING_BETA F-actin capping protein beta subunit signature. CDYNRD
ChainResidueDetails
JCYS62-ASP67
site_idPS00406
Number of Residues11
DetailsACTINS_1 Actins signature 1. YVGDEAQs.KRG
ChainResidueDetails
HTYR53-GLY63
site_idPS00432
Number of Residues9
DetailsACTINS_2 Actins signature 2. WITKqEYDE
ChainResidueDetails
HTRP356-GLU364
site_idPS00748
Number of Residues9
DetailsF_ACTIN_CAPPING_A_1 F-actin capping protein alpha subunit signature 1. VHYYEDGNV
ChainResidueDetails
IVAL196-VAL204
site_idPS00749
Number of Residues11
DetailsF_ACTIN_CAPPING_A_2 F-actin capping protein alpha subunit signature 2. KaLRRqLPVTR
ChainResidueDetails
ILYS256-ARG266
site_idPS01132
Number of Residues13
DetailsACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEPpLNTpeNR
ChainResidueDetails
ALEU111-ARG123
HLEU104-ARG116
BLEU108-ARG120
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P61158","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues11
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15505213","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17499050","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P61160","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues39
DetailsRepeat: {"description":"WD 1"}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues39
DetailsRepeat: {"description":"WD 2"}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues39
DetailsRepeat: {"description":"WD 3"}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues39
DetailsRepeat: {"description":"WD 4"}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues40
DetailsRepeat: {"description":"WD 5"}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"O15144","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"O15145","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"O15145","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"UniProtKB","id":"O15145","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues25
DetailsRegion: {"description":"Interaction with alpha-actinin","evidences":[{"source":"PubMed","id":"8449927","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues1
DetailsModified residue: {"description":"N6-malonyllysine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues1
DetailsModified residue: {"description":"Tele-methylhistidine","evidences":[{"source":"PubMed","id":"1150665","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16905096","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"213279","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2395459","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"499690","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1ATN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NWK","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues1
DetailsModified residue: {"description":"N6-methyllysine","evidences":[{"source":"UniProtKB","id":"P68133","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues1
DetailsModified residue: {"description":"ADP-ribosylarginine; by SpvB","evidences":[{"source":"PubMed","id":"16905096","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues3
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues3
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

248335

PDB entries from 2026-01-28

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