Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8V0Y

The structure of the native cardiac thin filament troponin core in Ca2+-free state from the upper strand activated by the C1-domain of cardiac myosin binding protein C

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000146	molecular_function	microfilament motor activity
A	0000166	molecular_function	nucleotide binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005856	cellular_component	cytoskeleton
A	0005884	cellular_component	actin filament
A	0017022	molecular_function	myosin binding
A	0030017	cellular_component	sarcomere
A	0030048	biological_process	actin filament-based movement
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	0043066	biological_process	negative regulation of apoptotic process
A	0045202	cellular_component	synapse
A	0055003	biological_process	cardiac myofibril assembly
A	0055008	biological_process	cardiac muscle tissue morphogenesis
A	0060047	biological_process	heart contraction
A	0060327	biological_process	cytoplasmic actin-based contraction involved in cell motility
A	0098978	cellular_component	glutamatergic synapse
B	0000146	molecular_function	microfilament motor activity
B	0000166	molecular_function	nucleotide binding
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0005856	cellular_component	cytoskeleton
B	0005884	cellular_component	actin filament
B	0017022	molecular_function	myosin binding
B	0030017	cellular_component	sarcomere
B	0030048	biological_process	actin filament-based movement
B	0030240	biological_process	skeletal muscle thin filament assembly
B	0031032	biological_process	actomyosin structure organization
B	0031674	cellular_component	I band
B	0033275	biological_process	actin-myosin filament sliding
B	0043066	biological_process	negative regulation of apoptotic process
B	0045202	cellular_component	synapse
B	0055003	biological_process	cardiac myofibril assembly
B	0055008	biological_process	cardiac muscle tissue morphogenesis
B	0060047	biological_process	heart contraction
B	0060327	biological_process	cytoplasmic actin-based contraction involved in cell motility
B	0098978	cellular_component	glutamatergic synapse
C	0003009	biological_process	skeletal muscle contraction
C	0005509	molecular_function	calcium ion binding
C	0005861	cellular_component	troponin complex
C	0006937	biological_process	regulation of muscle contraction
C	0008092	molecular_function	cytoskeletal protein binding
C	0014883	biological_process	transition between fast and slow fiber
C	0031013	molecular_function	troponin I binding
C	0031014	molecular_function	troponin T binding
C	0032972	biological_process	regulation of muscle filament sliding speed
C	0042803	molecular_function	protein homodimerization activity
C	0046872	molecular_function	metal ion binding
C	0048306	molecular_function	calcium-dependent protein binding
C	0051015	molecular_function	actin filament binding
C	0055010	biological_process	ventricular cardiac muscle tissue morphogenesis
C	0060048	biological_process	cardiac muscle contraction
C	0086003	biological_process	cardiac muscle cell contraction
C	1990584	cellular_component	cardiac Troponin complex
D	0003779	molecular_function	actin binding
D	0005861	cellular_component	troponin complex
E	0005861	cellular_component	troponin complex
E	0006937	biological_process	regulation of muscle contraction
F	0003779	molecular_function	actin binding
F	0005856	cellular_component	cytoskeleton
F	0005884	cellular_component	actin filament
F	0007015	biological_process	actin filament organization
F	0015629	cellular_component	actin cytoskeleton
F	0042802	molecular_function	identical protein binding
F	0042803	molecular_function	protein homodimerization activity
F	0046982	molecular_function	protein heterodimerization activity
F	0051015	molecular_function	actin filament binding
F	0060048	biological_process	cardiac muscle contraction
G	0003779	molecular_function	actin binding
G	0005856	cellular_component	cytoskeleton
G	0005884	cellular_component	actin filament
G	0007015	biological_process	actin filament organization
G	0015629	cellular_component	actin cytoskeleton
G	0042802	molecular_function	identical protein binding
G	0042803	molecular_function	protein homodimerization activity
G	0046982	molecular_function	protein heterodimerization activity
G	0051015	molecular_function	actin filament binding
G	0060048	biological_process	cardiac muscle contraction

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
C	ASP65-PHE77
C	ASP105-LEU117
C	ASP141-PHE153

site_id	PS00326
Number of Residues	9
Details	TROPOMYOSIN Tropomyosins signature. LKEAEtRAE

Chain	Residue	Details
F	LEU232-GLU240

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. WISKqEYDE

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	35
Details	Domain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	35
Details	Domain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	35
Details	Domain: {"description":"EF-hand 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	33
Details	Domain: {"description":"EF-hand 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	15
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P19123","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P09493","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P58771","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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