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8VO9

Cryo-EM structure of fascin crosslinked F-actin (Eigen_middle)

Functional Information from GO Data
ChainGOidnamespacecontents
A0001725cellular_componentstress fiber
A0001726cellular_componentruffle
A0002102cellular_componentpodosome
A0003723molecular_functionRNA binding
A0003779molecular_functionactin binding
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0005902cellular_componentmicrovillus
A0005911cellular_componentcell-cell junction
A0005938cellular_componentcell cortex
A0007015biological_processactin filament organization
A0007043biological_processcell-cell junction assembly
A0007163biological_processestablishment or maintenance of cell polarity
A0008144molecular_functionobsolete drug binding
A0010592biological_processpositive regulation of lamellipodium assembly
A0015629cellular_componentactin cytoskeleton
A0016477biological_processcell migration
A0030027cellular_componentlamellipodium
A0030035biological_processmicrospike assembly
A0030036biological_processactin cytoskeleton organization
A0030046biological_processparallel actin filament bundle assembly
A0030175cellular_componentfilopodium
A0030426cellular_componentgrowth cone
A0030674molecular_functionprotein-macromolecule adaptor activity
A0031252cellular_componentcell leading edge
A0031253cellular_componentcell projection membrane
A0032534biological_processregulation of microvillus assembly
A0032956biological_processregulation of actin cytoskeleton organization
A0035089biological_processestablishment of apical/basal cell polarity
A0042995cellular_componentcell projection
A0044393cellular_componentmicrospike
A0045296molecular_functioncadherin binding
A0048870biological_processcell motility
A0051015molecular_functionactin filament binding
A0051017biological_processactin filament bundle assembly
A0051491biological_processpositive regulation of filopodium assembly
A0070062cellular_componentextracellular exosome
A0070161cellular_componentanchoring junction
A0071803biological_processpositive regulation of podosome assembly
A0090091biological_processpositive regulation of extracellular matrix disassembly
B0000166molecular_functionnucleotide binding
B0001725cellular_componentstress fiber
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005856cellular_componentcytoskeleton
B0005865cellular_componentstriated muscle thin filament
B0005884cellular_componentactin filament
B0015629cellular_componentactin cytoskeleton
B0016787molecular_functionhydrolase activity
B0030240biological_processskeletal muscle thin filament assembly
B0048741biological_processskeletal muscle fiber development
C0000166molecular_functionnucleotide binding
C0001725cellular_componentstress fiber
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0005856cellular_componentcytoskeleton
C0005865cellular_componentstriated muscle thin filament
C0005884cellular_componentactin filament
C0015629cellular_componentactin cytoskeleton
C0016787molecular_functionhydrolase activity
C0030240biological_processskeletal muscle thin filament assembly
C0048741biological_processskeletal muscle fiber development
D0000166molecular_functionnucleotide binding
D0001725cellular_componentstress fiber
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0005856cellular_componentcytoskeleton
D0005865cellular_componentstriated muscle thin filament
D0005884cellular_componentactin filament
D0015629cellular_componentactin cytoskeleton
D0016787molecular_functionhydrolase activity
D0030240biological_processskeletal muscle thin filament assembly
D0048741biological_processskeletal muscle fiber development
E0000166molecular_functionnucleotide binding
E0001725cellular_componentstress fiber
E0005515molecular_functionprotein binding
E0005524molecular_functionATP binding
E0005737cellular_componentcytoplasm
E0005856cellular_componentcytoskeleton
E0005865cellular_componentstriated muscle thin filament
E0005884cellular_componentactin filament
E0015629cellular_componentactin cytoskeleton
E0016787molecular_functionhydrolase activity
E0030240biological_processskeletal muscle thin filament assembly
E0048741biological_processskeletal muscle fiber development
F0000166molecular_functionnucleotide binding
F0001725cellular_componentstress fiber
F0005515molecular_functionprotein binding
F0005524molecular_functionATP binding
F0005737cellular_componentcytoplasm
F0005856cellular_componentcytoskeleton
F0005865cellular_componentstriated muscle thin filament
F0005884cellular_componentactin filament
F0015629cellular_componentactin cytoskeleton
F0016787molecular_functionhydrolase activity
F0030240biological_processskeletal muscle thin filament assembly
F0048741biological_processskeletal muscle fiber development
G0000166molecular_functionnucleotide binding
G0001725cellular_componentstress fiber
G0005515molecular_functionprotein binding
G0005524molecular_functionATP binding
G0005737cellular_componentcytoplasm
G0005856cellular_componentcytoskeleton
G0005865cellular_componentstriated muscle thin filament
G0005884cellular_componentactin filament
G0015629cellular_componentactin cytoskeleton
G0016787molecular_functionhydrolase activity
G0030240biological_processskeletal muscle thin filament assembly
G0048741biological_processskeletal muscle fiber development
Functional Information from PROSITE/UniProt
site_idPS00406
Number of Residues11
DetailsACTINS_1 Actins signature 1. YVGDEAQs.KRG
ChainResidueDetails
BTYR53-GLY63

site_idPS00432
Number of Residues9
DetailsACTINS_2 Actins signature 2. WITKqEYDE
ChainResidueDetails
BTRP356-GLU364

site_idPS01132
Number of Residues13
DetailsACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR
ChainResidueDetails
BLEU104-ARG116

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsMOD_RES: Methionine (R)-sulfoxide => ECO:0000250|UniProtKB:P68134
ChainResidueDetails
BMET44
FMET47
GMET44
GMET47
BMET47
CMET44
CMET47
DMET44
DMET47
EMET44
EMET47
FMET44

site_idSWS_FT_FI2
Number of Residues6
DetailsMOD_RES: Tele-methylhistidine => ECO:0000269|PubMed:12356759, ECO:0007744|PDB:1MDU
ChainResidueDetails
BHIC73
CHIC73
DHIC73
EHIC73
FHIC73
GHIC73

site_idSWS_FT_FI3
Number of Residues6
DetailsMOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68133
ChainResidueDetails
BLYS84
CLYS84
DLYS84
ELYS84
FLYS84
GLYS84

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q61553
ChainResidueDetails
ALYS74

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER127
ASER234

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR239

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P85845
ChainResidueDetails
ATHR403

site_idSWS_FT_FI8
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25218447
ChainResidueDetails
ALYS399

237423

PDB entries from 2025-06-11

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