Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8UZ0

Straight actin filament from Arp2/3 branch junction sample (ADP)

Functional Information from GO Data

Chain	GOid	namespace	contents
J	0000166	molecular_function	nucleotide binding
J	0001725	cellular_component	stress fiber
J	0005515	molecular_function	protein binding
J	0005524	molecular_function	ATP binding
J	0005737	cellular_component	cytoplasm
J	0005856	cellular_component	cytoskeleton
J	0005865	cellular_component	striated muscle thin filament
J	0005884	cellular_component	actin filament
J	0015629	cellular_component	actin cytoskeleton
J	0016787	molecular_function	hydrolase activity
J	0030240	biological_process	skeletal muscle thin filament assembly
J	0048741	biological_process	skeletal muscle fiber development
K	0000166	molecular_function	nucleotide binding
K	0001725	cellular_component	stress fiber
K	0005515	molecular_function	protein binding
K	0005524	molecular_function	ATP binding
K	0005737	cellular_component	cytoplasm
K	0005856	cellular_component	cytoskeleton
K	0005865	cellular_component	striated muscle thin filament
K	0005884	cellular_component	actin filament
K	0015629	cellular_component	actin cytoskeleton
K	0016787	molecular_function	hydrolase activity
K	0030240	biological_process	skeletal muscle thin filament assembly
K	0048741	biological_process	skeletal muscle fiber development
L	0000166	molecular_function	nucleotide binding
L	0001725	cellular_component	stress fiber
L	0005515	molecular_function	protein binding
L	0005524	molecular_function	ATP binding
L	0005737	cellular_component	cytoplasm
L	0005856	cellular_component	cytoskeleton
L	0005865	cellular_component	striated muscle thin filament
L	0005884	cellular_component	actin filament
L	0015629	cellular_component	actin cytoskeleton
L	0016787	molecular_function	hydrolase activity
L	0030240	biological_process	skeletal muscle thin filament assembly
L	0048741	biological_process	skeletal muscle fiber development
M	0000166	molecular_function	nucleotide binding
M	0001725	cellular_component	stress fiber
M	0005515	molecular_function	protein binding
M	0005524	molecular_function	ATP binding
M	0005737	cellular_component	cytoplasm
M	0005856	cellular_component	cytoskeleton
M	0005865	cellular_component	striated muscle thin filament
M	0005884	cellular_component	actin filament
M	0015629	cellular_component	actin cytoskeleton
M	0016787	molecular_function	hydrolase activity
M	0030240	biological_process	skeletal muscle thin filament assembly
M	0048741	biological_process	skeletal muscle fiber development
N	0000166	molecular_function	nucleotide binding
N	0001725	cellular_component	stress fiber
N	0005515	molecular_function	protein binding
N	0005524	molecular_function	ATP binding
N	0005737	cellular_component	cytoplasm
N	0005856	cellular_component	cytoskeleton
N	0005865	cellular_component	striated muscle thin filament
N	0005884	cellular_component	actin filament
N	0015629	cellular_component	actin cytoskeleton
N	0016787	molecular_function	hydrolase activity
N	0030240	biological_process	skeletal muscle thin filament assembly
N	0048741	biological_process	skeletal muscle fiber development
O	0000166	molecular_function	nucleotide binding
O	0001725	cellular_component	stress fiber
O	0005515	molecular_function	protein binding
O	0005524	molecular_function	ATP binding
O	0005737	cellular_component	cytoplasm
O	0005856	cellular_component	cytoskeleton
O	0005865	cellular_component	striated muscle thin filament
O	0005884	cellular_component	actin filament
O	0015629	cellular_component	actin cytoskeleton
O	0016787	molecular_function	hydrolase activity
O	0030240	biological_process	skeletal muscle thin filament assembly
O	0048741	biological_process	skeletal muscle fiber development
P	0000166	molecular_function	nucleotide binding
P	0001725	cellular_component	stress fiber
P	0005515	molecular_function	protein binding
P	0005524	molecular_function	ATP binding
P	0005737	cellular_component	cytoplasm
P	0005856	cellular_component	cytoskeleton
P	0005865	cellular_component	striated muscle thin filament
P	0005884	cellular_component	actin filament
P	0015629	cellular_component	actin cytoskeleton
P	0016787	molecular_function	hydrolase activity
P	0030240	biological_process	skeletal muscle thin filament assembly
P	0048741	biological_process	skeletal muscle fiber development
Q	0000166	molecular_function	nucleotide binding
Q	0001725	cellular_component	stress fiber
Q	0005515	molecular_function	protein binding
Q	0005524	molecular_function	ATP binding
Q	0005737	cellular_component	cytoplasm
Q	0005856	cellular_component	cytoskeleton
Q	0005865	cellular_component	striated muscle thin filament
Q	0005884	cellular_component	actin filament
Q	0015629	cellular_component	actin cytoskeleton
Q	0016787	molecular_function	hydrolase activity
Q	0030240	biological_process	skeletal muscle thin filament assembly
Q	0048741	biological_process	skeletal muscle fiber development
R	0000166	molecular_function	nucleotide binding
R	0001725	cellular_component	stress fiber
R	0005515	molecular_function	protein binding
R	0005524	molecular_function	ATP binding
R	0005737	cellular_component	cytoplasm
R	0005856	cellular_component	cytoskeleton
R	0005865	cellular_component	striated muscle thin filament
R	0005884	cellular_component	actin filament
R	0015629	cellular_component	actin cytoskeleton
R	0016787	molecular_function	hydrolase activity
R	0030240	biological_process	skeletal muscle thin filament assembly
R	0048741	biological_process	skeletal muscle fiber development

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
J	TYR53-GLY63

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

Chain	Residue	Details
J	TRP356-GLU364

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

Chain	Residue	Details
J	LEU104-ARG116

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	225
Details	Region: {"description":"Interaction with alpha-actinin","evidences":[{"source":"PubMed","id":"8449927","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	18
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	9
Details	Modified residue: {"description":"N6-malonyllysine","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	9
Details	Modified residue: {"description":"Tele-methylhistidine","evidences":[{"source":"PubMed","id":"12356759","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1MDU","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	9
Details	Modified residue: {"description":"N6-methyllysine","evidences":[{"source":"UniProtKB","id":"P68133","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	9
Details	Modified residue: {"description":"ADP-ribosylarginine; by SpvB","evidences":[{"source":"PubMed","id":"16905096","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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