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

8GSU

Crystal structure of human cardiac alpha actin (WT_ADP-Pi) in complex with fragmin F1 domain

Functional Information from GO Data
ChainGOidnamespacecontents
A0000146molecular_functionmicrofilament motor activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0005884cellular_componentactin filament
A0005925cellular_componentfocal adhesion
A0007015biological_processactin filament organization
A0010628biological_processpositive regulation of gene expression
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0017022molecular_functionmyosin binding
A0030017cellular_componentsarcomere
A0030027cellular_componentlamellipodium
A0030048biological_processactin filament-based movement
A0030175cellular_componentfilopodium
A0030240biological_processskeletal muscle thin filament assembly
A0031032biological_processactomyosin structure organization
A0031674cellular_componentI band
A0033275biological_processactin-myosin filament sliding
A0043066biological_processnegative regulation of apoptotic process
A0044297cellular_componentcell body
A0045202cellular_componentsynapse
A0055003biological_processcardiac myofibril assembly
A0055008biological_processcardiac muscle tissue morphogenesis
A0060047biological_processheart contraction
A0070062cellular_componentextracellular exosome
A0070252biological_processactin-mediated cell contraction
A0072562cellular_componentblood microparticle
A0090131biological_processmesenchyme migration
A0098978cellular_componentglutamatergic synapse
B0051015molecular_functionactin filament binding
Functional Information from PROSITE/UniProt
site_idPS00406
Number of Residues11
DetailsACTINS_1 Actins signature 1. YVGDEAQs.KRG
ChainResidueDetails
ATYR53-GLY63

site_idPS00432
Number of Residues9
DetailsACTINS_2 Actins signature 2. WISKqEYDE
ChainResidueDetails
ATRP356-GLU364

site_idPS01132
Number of Residues13
DetailsACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR
ChainResidueDetails
ALEU104-ARG116

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: Methionine (R)-sulfoxide => ECO:0000250|UniProtKB:P68033
ChainResidueDetails
AMET44
AMET47

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Tele-methylhistidine => ECO:0000269|PubMed:30626964
ChainResidueDetails
AHIC73

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-methyllysine => ECO:0000269|PubMed:23673617
ChainResidueDetails
ALYS84

site_idSWS_FT_FI4
Number of Residues1
DetailsCROSSLNK: Isoglutamyl lysine isopeptide (Lys-Glu) (interchain with E-272); by Vibrio toxins RtxA and VgrG1 => ECO:0000250|UniProtKB:P60709
ChainResidueDetails
ALYS50

site_idSWS_FT_FI5
Number of Residues2
DetailsCROSSLNK: Isoglutamyl lysine isopeptide (Glu-Lys) (interchain with K-52); by Vibrio toxins RtxA and VgrG1 => ECO:0000250|UniProtKB:P60709
ChainResidueDetails
AGLU270

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon