1C1G

CRYSTAL STRUCTURE OF TROPOMYOSIN AT 7 ANGSTROMS RESOLUTION IN THE SPERMINE-INDUCED CRYSTAL FORM

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003779	molecular_function	actin binding
A	0005737	cellular_component	cytoplasm
A	0005856	cellular_component	cytoskeleton
A	0005884	cellular_component	actin filament
A	0007015	biological_process	actin filament organization
A	0015629	cellular_component	actin cytoskeleton
A	0042802	molecular_function	identical protein binding
A	0042803	molecular_function	protein homodimerization activity
A	0046982	molecular_function	protein heterodimerization activity
A	0051015	molecular_function	actin filament binding
A	0060048	biological_process	cardiac muscle contraction
B	0003779	molecular_function	actin binding
B	0005737	cellular_component	cytoplasm
B	0005856	cellular_component	cytoskeleton
B	0005884	cellular_component	actin filament
B	0007015	biological_process	actin filament organization
B	0015629	cellular_component	actin cytoskeleton
B	0042802	molecular_function	identical protein binding
B	0042803	molecular_function	protein homodimerization activity
B	0046982	molecular_function	protein heterodimerization activity
B	0051015	molecular_function	actin filament binding
B	0060048	biological_process	cardiac muscle contraction
C	0003779	molecular_function	actin binding
C	0005737	cellular_component	cytoplasm
C	0005856	cellular_component	cytoskeleton
C	0005884	cellular_component	actin filament
C	0007015	biological_process	actin filament organization
C	0015629	cellular_component	actin cytoskeleton
C	0042802	molecular_function	identical protein binding
C	0042803	molecular_function	protein homodimerization activity
C	0046982	molecular_function	protein heterodimerization activity
C	0051015	molecular_function	actin filament binding
C	0060048	biological_process	cardiac muscle contraction
D	0003779	molecular_function	actin binding
D	0005737	cellular_component	cytoplasm
D	0005856	cellular_component	cytoskeleton
D	0005884	cellular_component	actin filament
D	0007015	biological_process	actin filament organization
D	0015629	cellular_component	actin cytoskeleton
D	0042802	molecular_function	identical protein binding
D	0042803	molecular_function	protein homodimerization activity
D	0046982	molecular_function	protein heterodimerization activity
D	0051015	molecular_function	actin filament binding
D	0060048	biological_process	cardiac muscle contraction

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU232-GLU240

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	MOD_RES: N-acetylmethionine => ECO:0000250|UniProtKB:P09493

Chain	Residue	Details
A	MET1
B	MET285
C	MET569
D	MET853

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site_id	SWS_FT_FI2
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P04692

Chain	Residue	Details
A	SER45
B	SER329
C	SER613
D	SER897

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site_id	SWS_FT_FI3
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P09493

Chain	Residue	Details
A	SER174
B	SER458
C	SER742
D	SER1026

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site_id	SWS_FT_FI4
Number of Residues	16
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P58771

Chain	Residue	Details
A	SER186
C	SER774
C	SER820
C	SER839
D	SER1038
D	SER1058
D	SER1104
D	SER1123
A	SER206
A	SER252
A	SER271
B	SER470
B	SER490
B	SER536
B	SER555
C	SER754

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site_id	SWS_FT_FI5
Number of Residues	4
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P04692

Chain	Residue	Details
A	TYR261
B	TYR545
C	TYR829
D	TYR1113

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site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: Phosphoserine; by DAPK1 => ECO:0000250|UniProtKB:P09493

Chain	Residue	Details
A	SER283
B	SER567
C	SER851
D	SER1135

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