Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

7R94

T-Plastin-F-actin complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0001725cellular_componentstress fiber
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005856cellular_componentcytoskeleton
A0005865cellular_componentstriated muscle thin filament
A0005884cellular_componentactin filament
A0016787molecular_functionhydrolase activity
A0030240biological_processskeletal muscle thin filament assembly
A0048741biological_processskeletal muscle fiber development
B0001725cellular_componentstress fiber
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005856cellular_componentcytoskeleton
B0005865cellular_componentstriated muscle thin filament
B0005884cellular_componentactin filament
B0016787molecular_functionhydrolase activity
B0030240biological_processskeletal muscle thin filament assembly
B0048741biological_processskeletal muscle fiber development
C0001725cellular_componentstress fiber
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0005856cellular_componentcytoskeleton
C0005865cellular_componentstriated muscle thin filament
C0005884cellular_componentactin filament
C0016787molecular_functionhydrolase activity
C0030240biological_processskeletal muscle thin filament assembly
C0048741biological_processskeletal muscle fiber development
D0001725cellular_componentstress fiber
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0005856cellular_componentcytoskeleton
D0005865cellular_componentstriated muscle thin filament
D0005884cellular_componentactin filament
D0016787molecular_functionhydrolase activity
D0030240biological_processskeletal muscle thin filament assembly
D0048741biological_processskeletal muscle fiber development
E0001725cellular_componentstress fiber
E0005515molecular_functionprotein binding
E0005524molecular_functionATP binding
E0005737cellular_componentcytoplasm
E0005856cellular_componentcytoskeleton
E0005865cellular_componentstriated muscle thin filament
E0005884cellular_componentactin filament
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
F0005886cellular_componentplasma membrane
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
G0003779molecular_functionactin binding
G0005509molecular_functioncalcium ion binding
G0005737cellular_componentcytoplasm
G0005829cellular_componentcytosol
G0005884cellular_componentactin filament
G0005886cellular_componentplasma membrane
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
H0003779molecular_functionactin binding
H0005509molecular_functioncalcium ion binding
H0005737cellular_componentcytoplasm
H0005829cellular_componentcytosol
H0005884cellular_componentactin filament
H0005886cellular_componentplasma membrane
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
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 Residues27
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448
ChainResidueDetails
FASP25
GASP25
GASN27
GASN29
GGLU36
GASP65
GASN67
GASP69
GLYS71
GGLU76
HASP25
FASN27
HASN27
HASN29
HGLU36
HASP65
HASN67
HASP69
HLYS71
HGLU76
FASN29
FGLU36
FASP65
FASN67
FASP69
FLYS71
FGLU76

site_idSWS_FT_FI2
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q99K51
ChainResidueDetails
FSER268
GSER268
HSER268
DASP1
EASP1

site_idSWS_FT_FI3
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
FSER293
EMET47
GSER293
HSER293
BMET47
AMET44
AMET47
DMET44
DMET47
EMET44

site_idSWS_FT_FI4
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
FSER326
GSER326
HSER326
DHIC73
EHIC73

site_idSWS_FT_FI5
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
FSER339
GSER339
HSER339
DLYS84
ELYS84

site_idSWS_FT_FI6
Number of Residues3
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231
ChainResidueDetails
FTHR391
GTHR391
HTHR391

225681

PDB entries from 2024-10-02

PDB statisticsPDBj update infoContact PDBjnumon