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4A7F

Structure of the Actin-Tropomyosin-Myosin Complex (rigor ATM 3)

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
C0003774molecular_functioncytoskeletal motor activity
C0005524molecular_functionATP binding
C0016459cellular_componentmyosin complex
D0000166molecular_functionnucleotide binding
D0000287molecular_functionmagnesium ion binding
D0001725cellular_componentstress fiber
D0003785molecular_functionactin monomer binding
D0005509molecular_functioncalcium ion binding
D0005515molecular_functionprotein binding
D0005523molecular_functiontropomyosin binding
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0005856cellular_componentcytoskeleton
D0005865cellular_componentstriated muscle thin filament
D0005884cellular_componentactin filament
D0010628biological_processpositive regulation of gene expression
D0016787molecular_functionhydrolase activity
D0019904molecular_functionprotein domain specific binding
D0030027cellular_componentlamellipodium
D0030041biological_processactin filament polymerization
D0030175cellular_componentfilopodium
D0030240biological_processskeletal muscle thin filament assembly
D0031013molecular_functiontroponin I binding
D0031432molecular_functiontitin binding
D0031941cellular_componentfilamentous actin
D0032036molecular_functionmyosin heavy chain binding
D0032432cellular_componentactin filament bundle
D0042802molecular_functionidentical protein binding
D0044297cellular_componentcell body
D0048306molecular_functioncalcium-dependent protein binding
D0048741biological_processskeletal muscle fiber development
D0051017biological_processactin filament bundle assembly
D0090131biological_processmesenchyme migration
D0098723cellular_componentskeletal muscle myofibril
D0140660molecular_functioncytoskeletal motor activator activity
E0000166molecular_functionnucleotide binding
E0000287molecular_functionmagnesium ion binding
E0001725cellular_componentstress fiber
E0003785molecular_functionactin monomer binding
E0005509molecular_functioncalcium ion binding
E0005515molecular_functionprotein binding
E0005523molecular_functiontropomyosin binding
E0005524molecular_functionATP binding
E0005737cellular_componentcytoplasm
E0005856cellular_componentcytoskeleton
E0005865cellular_componentstriated muscle thin filament
E0005884cellular_componentactin filament
E0010628biological_processpositive regulation of gene expression
E0016787molecular_functionhydrolase activity
E0019904molecular_functionprotein domain specific binding
E0030027cellular_componentlamellipodium
E0030041biological_processactin filament polymerization
E0030175cellular_componentfilopodium
E0030240biological_processskeletal muscle thin filament assembly
E0031013molecular_functiontroponin I binding
E0031432molecular_functiontitin binding
E0031941cellular_componentfilamentous actin
E0032036molecular_functionmyosin heavy chain binding
E0032432cellular_componentactin filament bundle
E0042802molecular_functionidentical protein binding
E0044297cellular_componentcell body
E0048306molecular_functioncalcium-dependent protein binding
E0048741biological_processskeletal muscle fiber development
E0051017biological_processactin filament bundle assembly
E0090131biological_processmesenchyme migration
E0098723cellular_componentskeletal muscle myofibril
E0140660molecular_functioncytoskeletal motor activator activity
F0000166molecular_functionnucleotide binding
F0000287molecular_functionmagnesium ion binding
F0001725cellular_componentstress fiber
F0003785molecular_functionactin monomer binding
F0005509molecular_functioncalcium ion binding
F0005515molecular_functionprotein binding
F0005523molecular_functiontropomyosin binding
F0005524molecular_functionATP binding
F0005737cellular_componentcytoplasm
F0005856cellular_componentcytoskeleton
F0005865cellular_componentstriated muscle thin filament
F0005884cellular_componentactin filament
F0010628biological_processpositive regulation of gene expression
F0016787molecular_functionhydrolase activity
F0019904molecular_functionprotein domain specific binding
F0030027cellular_componentlamellipodium
F0030041biological_processactin filament polymerization
F0030175cellular_componentfilopodium
F0030240biological_processskeletal muscle thin filament assembly
F0031013molecular_functiontroponin I binding
F0031432molecular_functiontitin binding
F0031941cellular_componentfilamentous actin
F0032036molecular_functionmyosin heavy chain binding
F0032432cellular_componentactin filament bundle
F0042802molecular_functionidentical protein binding
F0044297cellular_componentcell body
F0048306molecular_functioncalcium-dependent protein binding
F0048741biological_processskeletal muscle fiber development
F0051017biological_processactin filament bundle assembly
F0090131biological_processmesenchyme migration
F0098723cellular_componentskeletal muscle myofibril
F0140660molecular_functioncytoskeletal motor activator activity
G0003774molecular_functioncytoskeletal motor activity
G0005524molecular_functionATP binding
G0016459cellular_componentmyosin complex
I0000166molecular_functionnucleotide binding
I0000287molecular_functionmagnesium ion binding
I0001725cellular_componentstress fiber
I0003785molecular_functionactin monomer binding
I0005509molecular_functioncalcium ion binding
I0005515molecular_functionprotein binding
I0005523molecular_functiontropomyosin binding
I0005524molecular_functionATP binding
I0005737cellular_componentcytoplasm
I0005856cellular_componentcytoskeleton
I0005865cellular_componentstriated muscle thin filament
I0005884cellular_componentactin filament
I0010628biological_processpositive regulation of gene expression
I0016787molecular_functionhydrolase activity
I0019904molecular_functionprotein domain specific binding
I0030027cellular_componentlamellipodium
I0030041biological_processactin filament polymerization
I0030175cellular_componentfilopodium
I0030240biological_processskeletal muscle thin filament assembly
I0031013molecular_functiontroponin I binding
I0031432molecular_functiontitin binding
I0031941cellular_componentfilamentous actin
I0032036molecular_functionmyosin heavy chain binding
I0032432cellular_componentactin filament bundle
I0042802molecular_functionidentical protein binding
I0044297cellular_componentcell body
I0048306molecular_functioncalcium-dependent protein binding
I0048741biological_processskeletal muscle fiber development
I0051017biological_processactin filament bundle assembly
I0090131biological_processmesenchyme migration
I0098723cellular_componentskeletal muscle myofibril
I0140660molecular_functioncytoskeletal motor activator activity
J0003774molecular_functioncytoskeletal motor activity
J0005524molecular_functionATP binding
J0016459cellular_componentmyosin complex
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ADP A 376
ChainResidue
AGLY13
AGLY302
AMET305
ALYS336
ACA377
ASER14
AGLY15
ALYS18
AGLY156
AASP157
AGLY158
AARG210
AGLU214

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CA A 377
ChainResidue
AGLN137
AADP376

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ADP D 376
ChainResidue
DGLY13
DSER14
DGLY15
DLYS18
DGLY156
DASP157
DGLY158
DARG210
DGLU214
DGLY302
DMET305
DLYS336
DCA377

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CA D 377
ChainResidue
DGLN137
DADP376

site_idAC5
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ADP E 376
ChainResidue
EGLY13
ESER14
EGLY15
ELYS18
EGLY156
EASP157
EGLY158
EARG210
EGLU214
EGLY302
EMET305
ELYS336
ECA377

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CA E 377
ChainResidue
EGLN137
EADP376

site_idAC7
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ADP F 376
ChainResidue
FGLY13
FSER14
FGLY15
FLYS18
FGLY156
FASP157
FGLY158
FARG210
FGLU214
FGLY302
FMET305
FLYS336
FCA377

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CA F 377
ChainResidue
FGLN137
FADP376

site_idAC9
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ADP I 376
ChainResidue
IGLY13
ISER14
IGLY15
ILYS18
IGLY156
IASP157
IGLY158
IARG210
IGLU214
IGLY302
IMET305
ILYS336
ICA377

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CA I 377
ChainResidue
IGLN137
IADP376

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. 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 Residues125
DetailsRegion: {"description":"Interaction with alpha-actinin","evidences":[{"source":"PubMed","id":"8449927","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues5
DetailsModified residue: {"description":"N-acetylaspartate; in Actin, alpha skeletal muscle","evidences":[{"source":"PubMed","id":"1150665","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues10
DetailsModified residue: {"description":"Methionine (R)-sulfoxide","evidences":[{"source":"UniProtKB","id":"P68134","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues5
DetailsModified residue: {"description":"N6-malonyllysine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues5
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_FI6
Number of Residues5
DetailsModified residue: {"description":"N6-methyllysine","evidences":[{"source":"UniProtKB","id":"P68133","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues5
DetailsModified residue: {"description":"ADP-ribosylarginine; by SpvB","evidences":[{"source":"PubMed","id":"16905096","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues109
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P09493","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P58771","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues222
DetailsRegion: {"description":"Actin-binding"}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues27
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues21
DetailsBinding site: {}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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