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

7SXA

T-Plastin-F-actin complex, pre-bundling intermediate state

Functional Information from GO Data
ChainGOidnamespacecontents
A0003779molecular_functionactin binding
A0005509molecular_functioncalcium ion binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005884cellular_componentactin filament
A0005886cellular_componentplasma membrane
A0032432cellular_componentactin filament bundle
A0046872molecular_functionmetal ion binding
A0051015molecular_functionactin filament binding
A0051017biological_processactin filament bundle assembly
A0051639biological_processactin filament network formation
A0060348biological_processbone 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
Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DLNSNGFICdyEL
ChainResidueDetails
AASP25-LEU37
AASP65-PHE77

site_idPS00019
Number of Residues10
DetailsACTININ_1 Actinin-type actin-binding domain signature 1. EKyAFVNWIN
ChainResidueDetails
AGLU125-ASN134
AGLU399-ASN408

site_idPS00020
Number of Residues25
DetailsACTININ_2 Actinin-type actin-binding domain signature 2. VvNIGAeDLrAgkphLvLGLLWqII
ChainResidueDetails
AVAL211-ILE235
ALEU478-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 Residues3
DetailsMOD_RES: N-acetylcysteine; in intermediate form => ECO:0000250|UniProtKB:P62737
ChainResidueDetails
CCYS0
BCYS0
DCYS0
AGLU36
AASP65
AASN67
AASP69
ALYS71
AGLU76

site_idSWS_FT_FI2
Number of Residues3
DetailsMOD_RES: N-acetylaspartate; in Actin, alpha skeletal muscle => ECO:0000269|PubMed:456601
ChainResidueDetails
CASP1
BASP1
DASP1

site_idSWS_FT_FI3
Number of Residues6
DetailsMOD_RES: Methionine (R)-sulfoxide => ECO:0000250|UniProtKB:P68134
ChainResidueDetails
CMET44
CMET47
BMET44
BMET47
DMET44
DMET47

site_idSWS_FT_FI4
Number of Residues3
DetailsMOD_RES: Tele-methylhistidine => ECO:0000269|PubMed:12356759, ECO:0007744|PDB:1MDU
ChainResidueDetails
CHIC73
BHIC73
DHIC73

site_idSWS_FT_FI5
Number of Residues3
DetailsMOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68133
ChainResidueDetails
CLYS84
BLYS84
DLYS84

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231
ChainResidueDetails
ATHR391

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon