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9JUS

Structure of villin bound to an actin trimer

Functional Information from GO Data
ChainGOidnamespacecontents
f0000166molecular_functionnucleotide binding
f0001725cellular_componentstress fiber
f0005200molecular_functionstructural constituent of cytoskeleton
f0005515molecular_functionprotein binding
f0005524molecular_functionATP binding
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
F0000166molecular_functionnucleotide binding
F0001725cellular_componentstress fiber
F0005200molecular_functionstructural constituent of cytoskeleton
F0005515molecular_functionprotein binding
F0005524molecular_functionATP binding
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
g0005200molecular_functionstructural constituent of cytoskeleton
g0005515molecular_functionprotein binding
g0005524molecular_functionATP binding
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
G0000166molecular_functionnucleotide binding
G0001725cellular_componentstress fiber
G0005200molecular_functionstructural constituent of cytoskeleton
G0005515molecular_functionprotein binding
G0005524molecular_functionATP binding
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
p0000166molecular_functionnucleotide binding
p0001725cellular_componentstress fiber
p0005200molecular_functionstructural constituent of cytoskeleton
p0005515molecular_functionprotein binding
p0005524molecular_functionATP binding
p0005856cellular_componentcytoskeleton
p0005865cellular_componentstriated muscle thin filament
p0005884cellular_componentactin filament
p0015629cellular_componentactin cytoskeleton
p0016787molecular_functionhydrolase activity
p0030240biological_processskeletal muscle thin filament assembly
p0048741biological_processskeletal muscle fiber development
P0000166molecular_functionnucleotide binding
P0001725cellular_componentstress fiber
P0005200molecular_functionstructural constituent of cytoskeleton
P0005515molecular_functionprotein binding
P0005524molecular_functionATP binding
P0005856cellular_componentcytoskeleton
P0005865cellular_componentstriated muscle thin filament
P0005884cellular_componentactin filament
P0015629cellular_componentactin cytoskeleton
P0016787molecular_functionhydrolase activity
P0030240biological_processskeletal muscle thin filament assembly
P0048741biological_processskeletal muscle fiber development
Functional Information from PROSITE/UniProt
site_idPS00406
Number of Residues11
DetailsACTINS_1 Actins signature 1. YVGDEAQs.KRG
ChainResidueDetails
pTYR53-GLY63

site_idPS00432
Number of Residues9
DetailsACTINS_2 Actins signature 2. WITKqEYDE
ChainResidueDetails
pTRP356-GLU364

site_idPS01132
Number of Residues13
DetailsACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR
ChainResidueDetails
pLEU104-ARG116

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsModified residue: {"description":"Methionine (R)-sulfoxide","evidences":[{"source":"UniProtKB","id":"P68134","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsModified residue: {"description":"Tele-methylhistidine","evidences":[{"source":"PubMed","id":"12356759","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1MDU","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsModified residue: {"description":"N6-methyllysine","evidences":[{"source":"UniProtKB","id":"P68133","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

250835

PDB entries from 2026-03-18

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