Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1J1E

Crystal structure of the 52kDa domain of human cardiac troponin in the Ca2+ saturated form

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0002086	biological_process	diaphragm contraction
A	0003009	biological_process	skeletal muscle contraction
A	0005509	molecular_function	calcium ion binding
A	0005515	molecular_function	protein binding
A	0005829	cellular_component	cytosol
A	0005861	cellular_component	troponin complex
A	0006937	biological_process	regulation of muscle contraction
A	0010038	biological_process	response to metal ion
A	0014883	biological_process	transition between fast and slow fiber
A	0030017	cellular_component	sarcomere
A	0030049	biological_process	muscle filament sliding
A	0031013	molecular_function	troponin I binding
A	0031014	molecular_function	troponin T binding
A	0032972	biological_process	regulation of muscle filament sliding speed
A	0042803	molecular_function	protein homodimerization activity
A	0043292	cellular_component	contractile muscle fiber
A	0043462	biological_process	regulation of ATP-dependent activity
A	0046872	molecular_function	metal ion binding
A	0048306	molecular_function	calcium-dependent protein binding
A	0051015	molecular_function	actin filament binding
A	0055010	biological_process	ventricular cardiac muscle tissue morphogenesis
A	0060048	biological_process	cardiac muscle contraction
A	1990584	cellular_component	cardiac Troponin complex
B	0005861	cellular_component	troponin complex
B	0006937	biological_process	regulation of muscle contraction
C	0005861	cellular_component	troponin complex
D	0002086	biological_process	diaphragm contraction
D	0003009	biological_process	skeletal muscle contraction
D	0005509	molecular_function	calcium ion binding
D	0005515	molecular_function	protein binding
D	0005829	cellular_component	cytosol
D	0005861	cellular_component	troponin complex
D	0006937	biological_process	regulation of muscle contraction
D	0010038	biological_process	response to metal ion
D	0014883	biological_process	transition between fast and slow fiber
D	0030017	cellular_component	sarcomere
D	0030049	biological_process	muscle filament sliding
D	0031013	molecular_function	troponin I binding
D	0031014	molecular_function	troponin T binding
D	0032972	biological_process	regulation of muscle filament sliding speed
D	0042803	molecular_function	protein homodimerization activity
D	0043292	cellular_component	contractile muscle fiber
D	0043462	biological_process	regulation of ATP-dependent activity
D	0046872	molecular_function	metal ion binding
D	0048306	molecular_function	calcium-dependent protein binding
D	0051015	molecular_function	actin filament binding
D	0055010	biological_process	ventricular cardiac muscle tissue morphogenesis
D	0060048	biological_process	cardiac muscle contraction
D	1990584	cellular_component	cardiac Troponin complex
E	0005861	cellular_component	troponin complex
E	0006937	biological_process	regulation of muscle contraction
F	0005861	cellular_component	troponin complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 201

Chain	Residue
A	ASP65
A	ASP67
A	SER69
A	THR71
A	ASP73
A	GLU76

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 202

Chain	Residue
A	TYR111
A	ASP113
A	GLU116
A	ASP105
A	ASN107
A	ASP109

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA A 203

Chain	Residue
A	ASP141
A	ASN143
A	ASP145
A	ARG147
A	GLU152

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA D 201

Chain	Residue
D	ASP65
D	ASP67
D	SER69
D	THR71
D	ASP73
D	GLU76

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA D 202

Chain	Residue
D	ASP105
D	ASN107
D	ASP109
D	TYR111
D	GLU116

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA D 203

Chain	Residue
D	ASP141
D	ASN143
D	ASP145
D	ARG147
D	GLU152

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
A	ASP65-PHE77
A	ASP105-LEU117
A	ASP141-PHE153

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	SITE: Involved in TNI-TNT interactions

Chain	Residue	Details
C	GLN81
A	GLU116
A	ASP141
A	ASN143
A	ASP145
A	ARG147
A	GLU152
D	ASP65
D	ASP67
D	SER69
D	THR71
C	ARG98
D	GLU76
D	ASP105
D	ASN107
D	ASP109
D	TYR111
D	GLU116
D	ASP141
D	ASN143
D	ASP145
D	ARG147
F	GLN81
D	GLU152
F	ARG98
A	GLU76
A	ASP105
A	ASN107
A	ASP109
A	TYR111

site_id	SWS_FT_FI2
Number of Residues	4
Details	MOD_RES: Phosphothreonine; by STK4/MST1 => ECO:0000269\|PubMed:18986304

Chain	Residue	Details
C	GLU32
C	GLN130
F	GLU32
F	GLN130

site_id	SWS_FT_FI3
Number of Residues	4
Details	MOD_RES: Phosphoserine; by PKC/PRKCE => ECO:0000250\|UniProtKB:P48787

Chain	Residue	Details
C	ALA43
C	ARG45
F	ALA43
F	ARG45

site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: Phosphothreonine; by STK4/MST1 => ECO:0000269\|PubMed:18986304, ECO:0000269\|PubMed:22972900

Chain	Residue	Details
C	LEU52
C	LEU144
F	LEU52
F	LEU144

site_id	SWS_FT_FI5
Number of Residues	6
Details	MOD_RES: Phosphoserine => ECO:0000269\|PubMed:22972900

Chain	Residue	Details
C	THR78
C	LEU167
C	GLY200
F	THR78
F	LEU167
F	GLY200

site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: Phosphothreonine => ECO:0000269\|PubMed:22972900

Chain	Residue	Details
C	ARG79
C	GLU182
F	ARG79
F	GLU182

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: Phosphoserine; by PAK3 => ECO:0000269\|PubMed:12242269

Chain	Residue	Details
C	ALA151
F	ALA151

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)