Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

9DUV

Cryo-EM structure of recombinant R254H ACTA1 phalloidin-stabilized F-actin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0001725	cellular_component	stress fiber
A	0005200	molecular_function	structural constituent of cytoskeleton
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005615	cellular_component	extracellular space
A	0005829	cellular_component	cytosol
A	0005856	cellular_component	cytoskeleton
A	0005865	cellular_component	striated muscle thin filament
A	0005884	cellular_component	actin filament
A	0006936	biological_process	muscle contraction
A	0010628	biological_process	positive regulation of gene expression
A	0015629	cellular_component	actin cytoskeleton
A	0016787	molecular_function	hydrolase activity
A	0017022	molecular_function	myosin binding
A	0030017	cellular_component	sarcomere
A	0030027	cellular_component	lamellipodium
A	0030175	cellular_component	filopodium
A	0030240	biological_process	skeletal muscle thin filament assembly
A	0043531	molecular_function	ADP binding
A	0044297	cellular_component	cell body
A	0048741	biological_process	skeletal muscle fiber development
A	0070062	cellular_component	extracellular exosome
A	0072562	cellular_component	blood microparticle
A	0090131	biological_process	mesenchyme migration
B	0000166	molecular_function	nucleotide binding
B	0001725	cellular_component	stress fiber
B	0005200	molecular_function	structural constituent of cytoskeleton
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005615	cellular_component	extracellular space
B	0005829	cellular_component	cytosol
B	0005856	cellular_component	cytoskeleton
B	0005865	cellular_component	striated muscle thin filament
B	0005884	cellular_component	actin filament
B	0006936	biological_process	muscle contraction
B	0010628	biological_process	positive regulation of gene expression
B	0015629	cellular_component	actin cytoskeleton
B	0016787	molecular_function	hydrolase activity
B	0017022	molecular_function	myosin binding
B	0030017	cellular_component	sarcomere
B	0030027	cellular_component	lamellipodium
B	0030175	cellular_component	filopodium
B	0030240	biological_process	skeletal muscle thin filament assembly
B	0043531	molecular_function	ADP binding
B	0044297	cellular_component	cell body
B	0048741	biological_process	skeletal muscle fiber development
B	0070062	cellular_component	extracellular exosome
B	0072562	cellular_component	blood microparticle
B	0090131	biological_process	mesenchyme migration
C	0000166	molecular_function	nucleotide binding
C	0001725	cellular_component	stress fiber
C	0005200	molecular_function	structural constituent of cytoskeleton
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005615	cellular_component	extracellular space
C	0005829	cellular_component	cytosol
C	0005856	cellular_component	cytoskeleton
C	0005865	cellular_component	striated muscle thin filament
C	0005884	cellular_component	actin filament
C	0006936	biological_process	muscle contraction
C	0010628	biological_process	positive regulation of gene expression
C	0015629	cellular_component	actin cytoskeleton
C	0016787	molecular_function	hydrolase activity
C	0017022	molecular_function	myosin binding
C	0030017	cellular_component	sarcomere
C	0030027	cellular_component	lamellipodium
C	0030175	cellular_component	filopodium
C	0030240	biological_process	skeletal muscle thin filament assembly
C	0043531	molecular_function	ADP binding
C	0044297	cellular_component	cell body
C	0048741	biological_process	skeletal muscle fiber development
C	0070062	cellular_component	extracellular exosome
C	0072562	cellular_component	blood microparticle
C	0090131	biological_process	mesenchyme migration
D	0000166	molecular_function	nucleotide binding
D	0001725	cellular_component	stress fiber
D	0005200	molecular_function	structural constituent of cytoskeleton
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0005615	cellular_component	extracellular space
D	0005829	cellular_component	cytosol
D	0005856	cellular_component	cytoskeleton
D	0005865	cellular_component	striated muscle thin filament
D	0005884	cellular_component	actin filament
D	0006936	biological_process	muscle contraction
D	0010628	biological_process	positive regulation of gene expression
D	0015629	cellular_component	actin cytoskeleton
D	0016787	molecular_function	hydrolase activity
D	0017022	molecular_function	myosin binding
D	0030017	cellular_component	sarcomere
D	0030027	cellular_component	lamellipodium
D	0030175	cellular_component	filopodium
D	0030240	biological_process	skeletal muscle thin filament assembly
D	0043531	molecular_function	ADP binding
D	0044297	cellular_component	cell body
D	0048741	biological_process	skeletal muscle fiber development
D	0070062	cellular_component	extracellular exosome
D	0072562	cellular_component	blood microparticle
D	0090131	biological_process	mesenchyme migration
E	0000166	molecular_function	nucleotide binding
E	0001725	cellular_component	stress fiber
E	0005200	molecular_function	structural constituent of cytoskeleton
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0005615	cellular_component	extracellular space
E	0005829	cellular_component	cytosol
E	0005856	cellular_component	cytoskeleton
E	0005865	cellular_component	striated muscle thin filament
E	0005884	cellular_component	actin filament
E	0006936	biological_process	muscle contraction
E	0010628	biological_process	positive regulation of gene expression
E	0015629	cellular_component	actin cytoskeleton
E	0016787	molecular_function	hydrolase activity
E	0017022	molecular_function	myosin binding
E	0030017	cellular_component	sarcomere
E	0030027	cellular_component	lamellipodium
E	0030175	cellular_component	filopodium
E	0030240	biological_process	skeletal muscle thin filament assembly
E	0043531	molecular_function	ADP binding
E	0044297	cellular_component	cell body
E	0048741	biological_process	skeletal muscle fiber development
E	0070062	cellular_component	extracellular exosome
E	0072562	cellular_component	blood microparticle
E	0090131	biological_process	mesenchyme migration
F	0000166	molecular_function	nucleotide binding
F	0001725	cellular_component	stress fiber
F	0005200	molecular_function	structural constituent of cytoskeleton
F	0005515	molecular_function	protein binding
F	0005524	molecular_function	ATP binding
F	0005615	cellular_component	extracellular space
F	0005829	cellular_component	cytosol
F	0005856	cellular_component	cytoskeleton
F	0005865	cellular_component	striated muscle thin filament
F	0005884	cellular_component	actin filament
F	0006936	biological_process	muscle contraction
F	0010628	biological_process	positive regulation of gene expression
F	0015629	cellular_component	actin cytoskeleton
F	0016787	molecular_function	hydrolase activity
F	0017022	molecular_function	myosin binding
F	0030017	cellular_component	sarcomere
F	0030027	cellular_component	lamellipodium
F	0030175	cellular_component	filopodium
F	0030240	biological_process	skeletal muscle thin filament assembly
F	0043531	molecular_function	ADP binding
F	0044297	cellular_component	cell body
F	0048741	biological_process	skeletal muscle fiber development
F	0070062	cellular_component	extracellular exosome
F	0072562	cellular_component	blood microparticle
F	0090131	biological_process	mesenchyme migration

Functional Information from PROSITE/UniProt

site_id	PS00406
Number of Residues	11
Details	ACTINS_1 Actins signature 1. YVGDEAQs.KRG

Chain	Residue	Details
A	TYR53-GLY63

site_id	PS00432
Number of Residues	9
Details	ACTINS_2 Actins signature 2. WITKqEYDE

Chain	Residue	Details
A	TRP356-GLU364

site_id	PS01132
Number of Residues	13
Details	ACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR

Chain	Residue	Details
A	LEU104-ARG116

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	150
Details	Region: {"description":"Interaction with alpha-actinin","evidences":[{"source":"UniProtKB","id":"P68135","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	12
Details	Modified residue: {"description":"Methionine (R)-sulfoxide","evidences":[{"source":"UniProtKB","id":"P68134","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	6
Details	Modified residue: {"description":"N6-malonyllysine","evidences":[{"source":"PubMed","id":"21908771","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	6
Details	Modified residue: {"description":"Tele-methylhistidine","evidences":[{"source":"PubMed","id":"30626964","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	6
Details	Modified residue: {"description":"N6-methyllysine","evidences":[{"source":"PubMed","id":"23673617","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	6
Details	Cross-link: {"description":"Isoglutamyl lysine isopeptide (Lys-Glu) (interchain with E-272); by Vibrio toxins RtxA and VgrG1","evidences":[{"source":"UniProtKB","id":"P60709","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	12
Details	Cross-link: {"description":"Isoglutamyl lysine isopeptide (Glu-Lys) (interchain with K-52); by Vibrio toxins RtxA and VgrG1","evidences":[{"source":"UniProtKB","id":"P60709","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)