8GSU

Crystal structure of human cardiac alpha actin (WT_ADP-Pi) in complex with fragmin F1 domain

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000146	molecular_function	microfilament motor activity
A	0000166	molecular_function	nucleotide binding
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	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005856	cellular_component	cytoskeleton
A	0005884	cellular_component	actin filament
A	0005925	cellular_component	focal adhesion
A	0007015	biological_process	actin filament organization
A	0009410	biological_process	response to xenobiotic stimulus
A	0010628	biological_process	positive regulation of gene expression
A	0015629	cellular_component	actin cytoskeleton
A	0016020	cellular_component	membrane
A	0016787	molecular_function	hydrolase activity
A	0017022	molecular_function	myosin binding
A	0030017	cellular_component	sarcomere
A	0030027	cellular_component	lamellipodium
A	0030048	biological_process	actin filament-based movement
A	0030175	cellular_component	filopodium
A	0030240	biological_process	skeletal muscle thin filament assembly
A	0031032	biological_process	actomyosin structure organization
A	0031674	cellular_component	I band
A	0033275	biological_process	actin-myosin filament sliding
A	0044297	cellular_component	cell body
A	0045202	cellular_component	synapse
A	0045471	biological_process	response to ethanol
A	0055003	biological_process	cardiac myofibril assembly
A	0055008	biological_process	cardiac muscle tissue morphogenesis
A	0060047	biological_process	heart contraction
A	0060048	biological_process	cardiac muscle contraction
A	0070062	cellular_component	extracellular exosome
A	0072562	cellular_component	blood microparticle
A	0090131	biological_process	mesenchyme migration
A	0098978	cellular_component	glutamatergic synapse
B	0051015	molecular_function	actin filament binding

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

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

Chain	Residue	Details
A	TRP356-GLU364

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

Chain	Residue	Details
A	LEU104-ARG116

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Modified residue: {"description":"Tele-methylhistidine","evidences":[{"source":"PubMed","id":"30626964","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	1
Details	Modified residue: {"description":"N6-methyllysine","evidences":[{"source":"PubMed","id":"23673617","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	1
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

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site_id	SWS_FT_FI4
Number of Residues	2
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

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