Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7SX9

T-Plastin-F-actin complex, anti-parallel bundled state

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	0005856	cellular_component	cytoskeleton
A	0005865	cellular_component	striated muscle thin filament
A	0005884	cellular_component	actin filament
A	0015629	cellular_component	actin cytoskeleton
A	0016787	molecular_function	hydrolase activity
A	0030240	biological_process	skeletal muscle thin filament assembly
A	0048741	biological_process	skeletal muscle fiber development
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	0005856	cellular_component	cytoskeleton
B	0005865	cellular_component	striated muscle thin filament
B	0005884	cellular_component	actin filament
B	0015629	cellular_component	actin cytoskeleton
B	0016787	molecular_function	hydrolase activity
B	0030240	biological_process	skeletal muscle thin filament assembly
B	0048741	biological_process	skeletal muscle fiber development
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	0005856	cellular_component	cytoskeleton
C	0005865	cellular_component	striated muscle thin filament
C	0005884	cellular_component	actin filament
C	0015629	cellular_component	actin cytoskeleton
C	0016787	molecular_function	hydrolase activity
C	0030240	biological_process	skeletal muscle thin filament assembly
C	0048741	biological_process	skeletal muscle fiber development
D	0003779	molecular_function	actin binding
D	0005509	molecular_function	calcium ion binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0005884	cellular_component	actin filament
D	0031594	cellular_component	neuromuscular junction
D	0032432	cellular_component	actin filament bundle
D	0046872	molecular_function	metal ion binding
D	0051015	molecular_function	actin filament binding
D	0051017	biological_process	actin filament bundle assembly
D	0051639	biological_process	actin filament network formation
D	0060348	biological_process	bone development
D	0098693	biological_process	regulation of synaptic vesicle cycle
D	0098699	molecular_function	structural constituent of presynaptic actin cytoskeleton
D	0099140	biological_process	presynaptic actin cytoskeleton organization
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	0005856	cellular_component	cytoskeleton
E	0005865	cellular_component	striated muscle thin filament
E	0005884	cellular_component	actin filament
E	0015629	cellular_component	actin cytoskeleton
E	0016787	molecular_function	hydrolase activity
E	0030240	biological_process	skeletal muscle thin filament assembly
E	0048741	biological_process	skeletal muscle fiber development
G	0000166	molecular_function	nucleotide binding
G	0001725	cellular_component	stress fiber
G	0005200	molecular_function	structural constituent of cytoskeleton
G	0005515	molecular_function	protein binding
G	0005524	molecular_function	ATP binding
G	0005856	cellular_component	cytoskeleton
G	0005865	cellular_component	striated muscle thin filament
G	0005884	cellular_component	actin filament
G	0015629	cellular_component	actin cytoskeleton
G	0016787	molecular_function	hydrolase activity
G	0030240	biological_process	skeletal muscle thin filament assembly
G	0048741	biological_process	skeletal muscle fiber development
H	0000166	molecular_function	nucleotide binding
H	0001725	cellular_component	stress fiber
H	0005200	molecular_function	structural constituent of cytoskeleton
H	0005515	molecular_function	protein binding
H	0005524	molecular_function	ATP binding
H	0005856	cellular_component	cytoskeleton
H	0005865	cellular_component	striated muscle thin filament
H	0005884	cellular_component	actin filament
H	0015629	cellular_component	actin cytoskeleton
H	0016787	molecular_function	hydrolase activity
H	0030240	biological_process	skeletal muscle thin filament assembly
H	0048741	biological_process	skeletal muscle fiber development

Functional Information from PROSITE/UniProt

site_id	PS00018
Number of Residues	13
Details	EF_HAND_1 EF-hand calcium-binding domain. DLNSNGFICdyEL

Chain	Residue	Details
D	ASP25-LEU37
D	ASP65-PHE77

site_id	PS00019
Number of Residues	10
Details	ACTININ_1 Actinin-type actin-binding domain signature 1. EKyAFVNWIN

Chain	Residue	Details
D	GLU125-ASN134
D	GLU399-ASN408

site_id	PS00020
Number of Residues	25
Details	ACTININ_2 Actinin-type actin-binding domain signature 2. VvNIGAeDLrAgkphLvLGLLWqII

Chain	Residue	Details
D	VAL211-ILE235
D	LEU478-MET502

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

Chain	Residue	Details
B	TYR53-GLY63

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

Chain	Residue	Details
B	TRP356-GLU364

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

Chain	Residue	Details
B	LEU104-ARG116

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
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_FI2
Number of Residues	6
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_FI3
Number of Residues	6
Details	Modified residue: {"description":"N6-methyllysine","evidences":[{"source":"UniProtKB","id":"P68133","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	116
Details	Domain: {"description":"Calponin-homology (CH) 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00044","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	109
Details	Domain: {"description":"Calponin-homology (CH) 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00044","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	109
Details	Domain: {"description":"Calponin-homology (CH) 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00044","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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