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7R94

T-Plastin-F-actin complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0001725cellular_componentstress fiber
A0005200molecular_functionstructural constituent of cytoskeleton
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005856cellular_componentcytoskeleton
A0005865cellular_componentstriated muscle thin filament
A0005884cellular_componentactin filament
A0015629cellular_componentactin cytoskeleton
A0016787molecular_functionhydrolase activity
A0030240biological_processskeletal muscle thin filament assembly
A0048741biological_processskeletal muscle fiber development
B0000166molecular_functionnucleotide binding
B0001725cellular_componentstress fiber
B0005200molecular_functionstructural constituent of cytoskeleton
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
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
C0005200molecular_functionstructural constituent of cytoskeleton
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
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
D0005200molecular_functionstructural constituent of cytoskeleton
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
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
E0005200molecular_functionstructural constituent of cytoskeleton
E0005515molecular_functionprotein binding
E0005524molecular_functionATP binding
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
F0003779molecular_functionactin binding
F0005509molecular_functioncalcium ion binding
F0005737cellular_componentcytoplasm
F0005829cellular_componentcytosol
F0005884cellular_componentactin filament
F0031594cellular_componentneuromuscular junction
F0032432cellular_componentactin filament bundle
F0046872molecular_functionmetal ion binding
F0051015molecular_functionactin filament binding
F0051017biological_processactin filament bundle assembly
F0051639biological_processactin filament network formation
F0060348biological_processbone development
F0098693biological_processregulation of synaptic vesicle cycle
F0098699molecular_functionstructural constituent of presynaptic actin cytoskeleton
F0099140biological_processpresynaptic actin cytoskeleton organization
G0003779molecular_functionactin binding
G0005509molecular_functioncalcium ion binding
G0005737cellular_componentcytoplasm
G0005829cellular_componentcytosol
G0005884cellular_componentactin filament
G0031594cellular_componentneuromuscular junction
G0032432cellular_componentactin filament bundle
G0046872molecular_functionmetal ion binding
G0051015molecular_functionactin filament binding
G0051017biological_processactin filament bundle assembly
G0051639biological_processactin filament network formation
G0060348biological_processbone development
G0098693biological_processregulation of synaptic vesicle cycle
G0098699molecular_functionstructural constituent of presynaptic actin cytoskeleton
G0099140biological_processpresynaptic actin cytoskeleton organization
H0003779molecular_functionactin binding
H0005509molecular_functioncalcium ion binding
H0005737cellular_componentcytoplasm
H0005829cellular_componentcytosol
H0005884cellular_componentactin filament
H0031594cellular_componentneuromuscular junction
H0032432cellular_componentactin filament bundle
H0046872molecular_functionmetal ion binding
H0051015molecular_functionactin filament binding
H0051017biological_processactin filament bundle assembly
H0051639biological_processactin filament network formation
H0060348biological_processbone development
H0098693biological_processregulation of synaptic vesicle cycle
H0098699molecular_functionstructural constituent of presynaptic actin cytoskeleton
H0099140biological_processpresynaptic actin cytoskeleton organization
Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DLNSNGFICdyEL
ChainResidueDetails
FASP25-LEU37
FASP65-PHE77

site_idPS00019
Number of Residues10
DetailsACTININ_1 Actinin-type actin-binding domain signature 1. EKyAFVNWIN
ChainResidueDetails
FGLU125-ASN134
FGLU399-ASN408

site_idPS00020
Number of Residues25
DetailsACTININ_2 Actinin-type actin-binding domain signature 2. VvNIGAeDLrAgkphLvLGLLWqII
ChainResidueDetails
FVAL211-ILE235
FLEU478-MET502

site_idPS00406
Number of Residues11
DetailsACTINS_1 Actins signature 1. YVGDEAQs.KRG
ChainResidueDetails
CTYR53-GLY63

site_idPS00432
Number of Residues9
DetailsACTINS_2 Actins signature 2. WITKqEYDE
ChainResidueDetails
CTRP356-GLU364

site_idPS01132
Number of Residues13
DetailsACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR
ChainResidueDetails
CLEU104-ARG116

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsModified residue: {"description":"Methionine (R)-sulfoxide","evidences":[{"source":"UniProtKB","id":"P68134","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues5
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 Residues5
DetailsModified residue: {"description":"N6-methyllysine","evidences":[{"source":"UniProtKB","id":"P68133","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues327
DetailsDomain: {"description":"Calponin-homology (CH) 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00044","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues327
DetailsDomain: {"description":"Calponin-homology (CH) 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00044","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues3
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

248335

PDB entries from 2026-01-28

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