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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

6NBE

Ternary Complex of Ac-Alpha-Actin with Profilin and CoA-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 Residues6
Detailsbinding site for residue CA A 400
ChainResidue
AATP401
AHOH520
AHOH524
AHOH543
AHOH544
AHOH564
site_idAC2
Number of Residues27
Detailsbinding site for residue ATP A 401
ChainResidue
ALEU16
ALYS18
AGLY156
AASP157
AGLY158
AVAL159
AGLY182
AARG210
ALYS213
AGLU214
AGLY301
AGLY302
ATHR303
AMET305
ATYR306
ALYS336
ACA400
AHOH522
AHOH543
AHOH562
AHOH564
AHOH584
AHOH623
AHOH628
AGLY13
ASER14
AGLY15
site_idAC3
Number of Residues12
Detailsbinding site for residue LAB A 402
ChainResidue
AGLY15
ALEU16
APRO32
AILE34
AGLN59
ATYR69
AASP157
AARG183
ATHR186
AARG206
AGLU207
AARG210
site_idAC4
Number of Residues6
Detailsbinding site for residue GOL A 403
ChainResidue
AHIC73
AARG183
AASP184
AHOH503
AHOH508
NTHR206
site_idAC5
Number of Residues5
Detailsbinding site for residue GOL A 404
ChainResidue
ATYR198
ASER199
APHE200
AGLU205
AHOH506
site_idAC6
Number of Residues31
Detailsbinding site for residue COA N 400
ChainResidue
AKKD1
AILE267
AGLY268
NALA74
NHIS76
NGLN104
NTRP105
NVAL163
NVAL164
NVAL165
NARG170
NGLY171
NARG172
NGLY173
NPHE174
NGLY175
NARG176
NTHR198
NGLN201
NPHE204
NTYR205
NHIS207
NHOH507
NHOH511
NHOH513
NHOH515
NHOH548
NHOH549
NHOH573
NHOH577
NHOH583
site_idAC7
Number of Residues10
Detailsbinding site for residue MES N 401
ChainResidue
ASER234
AGLU237
ALYS238
ASER239
NPHE123
NPRO155
NGLN156
NARG189
NGLY190
NPHE191
site_idAC8
Number of Residues7
Detailsbinding site for residue GOL N 402
ChainResidue
NALA166
NARG167
NHOH537
NHOH552
NHOH562
NLEU100
NASP103
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 Residues147
DetailsDomain: {"description":"N-acetyltransferase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00532","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q59DX8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P62963","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by ROCK1","evidences":[{"source":"PubMed","id":"18573880","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate"}
ChainResidueDetails

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PDB entries from 2026-01-14

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