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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

6NAS

Ternary Complex of Ac-Alpha-Actin with Profilin and AcCoA-NAA80

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0001725cellular_componentstress fiber
A0003785molecular_functionactin monomer binding
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005523molecular_functiontropomyosin binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005856cellular_componentcytoskeleton
A0005865cellular_componentstriated muscle thin filament
A0005884cellular_componentactin filament
A0010628biological_processpositive regulation of gene expression
A0016787molecular_functionhydrolase activity
A0019904molecular_functionprotein domain specific binding
A0030027cellular_componentlamellipodium
A0030041biological_processactin filament polymerization
A0030175cellular_componentfilopodium
A0030240biological_processskeletal muscle thin filament assembly
A0031013molecular_functiontroponin I binding
A0031432molecular_functiontitin binding
A0031941cellular_componentfilamentous actin
A0032036molecular_functionmyosin heavy chain binding
A0032432cellular_componentactin filament bundle
A0042802molecular_functionidentical protein binding
A0044297cellular_componentcell body
A0048306molecular_functioncalcium-dependent protein binding
A0048741biological_processskeletal muscle fiber development
A0051017biological_processactin filament bundle assembly
A0090131biological_processmesenchyme migration
A0098723cellular_componentskeletal muscle myofibril
A0140660molecular_functioncytoskeletal motor activator activity
N0008080molecular_functionN-acetyltransferase activity
N0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
P0000774molecular_functionadenyl-nucleotide exchange factor activity
P0001784molecular_functionphosphotyrosine residue binding
P0003723molecular_functionRNA binding
P0003779molecular_functionactin binding
P0003785molecular_functionactin monomer binding
P0005515molecular_functionprotein binding
P0005546molecular_functionphosphatidylinositol-4,5-bisphosphate binding
P0005634cellular_componentnucleus
P0005737cellular_componentcytoplasm
P0005829cellular_componentcytosol
P0005856cellular_componentcytoskeleton
P0005925cellular_componentfocal adhesion
P0005938cellular_componentcell cortex
P0010634biological_processpositive regulation of epithelial cell migration
P0016020cellular_componentmembrane
P0030036biological_processactin cytoskeleton organization
P0030833biological_processregulation of actin filament polymerization
P0030838biological_processpositive regulation of actin filament polymerization
P0031267molecular_functionsmall GTPase binding
P0032232biological_processnegative regulation of actin filament bundle assembly
P0032233biological_processpositive regulation of actin filament bundle assembly
P0045296molecular_functioncadherin binding
P0050804biological_processmodulation of chemical synaptic transmission
P0050821biological_processprotein stabilization
P0051497biological_processnegative regulation of stress fiber assembly
P0060074biological_processsynapse maturation
P0070062cellular_componentextracellular exosome
P0070064molecular_functionproline-rich region binding
P0072562cellular_componentblood microparticle
P0098885biological_processmodification of postsynaptic actin cytoskeleton
P0098978cellular_componentglutamatergic synapse
P0110053biological_processregulation of actin filament organization
P1900029biological_processpositive regulation of ruffle assembly
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue CA A 400
ChainResidue
AGLN137
AATP401
site_idAC2
Number of Residues19
Detailsbinding site for residue ATP A 401
ChainResidue
AASP157
AGLY158
AVAL159
AGLY182
ALYS213
AGLU214
AGLY301
AGLY302
ATHR303
ATYR306
ALYS336
ACA400
AGLY13
ASER14
AGLY15
ALEU16
ALYS18
AGLY74
AGLY156
site_idAC3
Number of Residues11
Detailsbinding site for residue LAB A 402
ChainResidue
AGLY15
ALEU16
AGLN59
AARG62
ATYR69
AASP157
AARG183
ATHR186
AARG206
AGLU207
AARG210
site_idAC4
Number of Residues4
Detailsbinding site for residue GOL A 403
ChainResidue
AHIC73
AARG183
AASP184
NTHR206
site_idAC5
Number of Residues3
Detailsbinding site for residue GOL A 404
ChainResidue
ASER199
AGLU205
AGLN246
site_idAC6
Number of Residues22
Detailsbinding site for residue ACO N 400
ChainResidue
AKKD1
AILE267
AGLY268
NGLY75
NHIS76
NGLN104
NVAL163
NVAL164
NVAL165
NARG170
NGLY171
NARG172
NGLY173
NPHE174
NGLY175
NARG176
NTHR198
NHIS199
NGLN201
NPHE204
NTYR205
NHIS207
site_idAC7
Number of Residues9
Detailsbinding site for residue MES N 401
ChainResidue
ASER234
AGLU237
ASER239
NPHE123
NARG150
NPRO155
NARG189
NGLY190
NPHE191
site_idAC8
Number of Residues3
Detailsbinding site for residue GOL N 402
ChainResidue
NASP103
NALA166
NARG167
Functional Information from PROSITE/UniProt
site_idPS00406
Number of Residues11
DetailsACTINS_1 Actins signature 1. YVGDEAQs.KRG
ChainResidueDetails
ATYR53-GLY63
site_idPS00414
Number of Residues9
DetailsPROFILIN Profilin signature. mAgWNaYiD
ChainResidueDetails
PMET0-ASP8
site_idPS00432
Number of Residues9
DetailsACTINS_2 Actins signature 2. WITKqEYDE
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 Residues13
DetailsRegion: {"description":"Interaction with alpha-actinin","evidences":[{"source":"PubMed","id":"8449927","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues2
DetailsModified residue: {"description":"Methionine (R)-sulfoxide","evidences":[{"source":"UniProtKB","id":"P68134","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"N6-malonyllysine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Tele-methylhistidine","evidences":[{"source":"PubMed","id":"1150665","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16905096","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"213279","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2395459","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"499690","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1ATN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NWK","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"N6-methyllysine","evidences":[{"source":"UniProtKB","id":"P68133","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"ADP-ribosylarginine; by SpvB","evidences":[{"source":"PubMed","id":"16905096","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q59DX8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P62963","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by ROCK1","evidences":[{"source":"PubMed","id":"18573880","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate"}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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