Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6T25

Cryo-EM structure of phalloidin-Alexa Flour-546-stabilized F-actin (copolymerized)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000287	molecular_function	magnesium ion binding
A	0001725	cellular_component	stress fiber
A	0003785	molecular_function	actin monomer binding
A	0005509	molecular_function	calcium ion binding
A	0005515	molecular_function	protein binding
A	0005523	molecular_function	tropomyosin binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005856	cellular_component	cytoskeleton
A	0005865	cellular_component	striated muscle thin filament
A	0005884	cellular_component	actin filament
A	0010628	biological_process	positive regulation of gene expression
A	0016787	molecular_function	hydrolase activity
A	0019904	molecular_function	protein domain specific binding
A	0030027	cellular_component	lamellipodium
A	0030041	biological_process	actin filament polymerization
A	0030175	cellular_component	filopodium
A	0030240	biological_process	skeletal muscle thin filament assembly
A	0031013	molecular_function	troponin I binding
A	0031432	molecular_function	titin binding
A	0031941	cellular_component	filamentous actin
A	0032036	molecular_function	myosin heavy chain binding
A	0032432	cellular_component	actin filament bundle
A	0042802	molecular_function	identical protein binding
A	0044297	cellular_component	cell body
A	0048306	molecular_function	calcium-dependent protein binding
A	0048741	biological_process	skeletal muscle fiber development
A	0051017	biological_process	actin filament bundle assembly
A	0090131	biological_process	mesenchyme migration
A	0098723	cellular_component	skeletal muscle myofibril
A	0140660	molecular_function	cytoskeletal motor activator activity
B	0000166	molecular_function	nucleotide binding
B	0000287	molecular_function	magnesium ion binding
B	0001725	cellular_component	stress fiber
B	0003785	molecular_function	actin monomer binding
B	0005509	molecular_function	calcium ion binding
B	0005515	molecular_function	protein binding
B	0005523	molecular_function	tropomyosin binding
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005856	cellular_component	cytoskeleton
B	0005865	cellular_component	striated muscle thin filament
B	0005884	cellular_component	actin filament
B	0010628	biological_process	positive regulation of gene expression
B	0016787	molecular_function	hydrolase activity
B	0019904	molecular_function	protein domain specific binding
B	0030027	cellular_component	lamellipodium
B	0030041	biological_process	actin filament polymerization
B	0030175	cellular_component	filopodium
B	0030240	biological_process	skeletal muscle thin filament assembly
B	0031013	molecular_function	troponin I binding
B	0031432	molecular_function	titin binding
B	0031941	cellular_component	filamentous actin
B	0032036	molecular_function	myosin heavy chain binding
B	0032432	cellular_component	actin filament bundle
B	0042802	molecular_function	identical protein binding
B	0044297	cellular_component	cell body
B	0048306	molecular_function	calcium-dependent protein binding
B	0048741	biological_process	skeletal muscle fiber development
B	0051017	biological_process	actin filament bundle assembly
B	0090131	biological_process	mesenchyme migration
B	0098723	cellular_component	skeletal muscle myofibril
B	0140660	molecular_function	cytoskeletal motor activator activity
C	0000166	molecular_function	nucleotide binding
C	0000287	molecular_function	magnesium ion binding
C	0001725	cellular_component	stress fiber
C	0003785	molecular_function	actin monomer binding
C	0005509	molecular_function	calcium ion binding
C	0005515	molecular_function	protein binding
C	0005523	molecular_function	tropomyosin binding
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0005856	cellular_component	cytoskeleton
C	0005865	cellular_component	striated muscle thin filament
C	0005884	cellular_component	actin filament
C	0010628	biological_process	positive regulation of gene expression
C	0016787	molecular_function	hydrolase activity
C	0019904	molecular_function	protein domain specific binding
C	0030027	cellular_component	lamellipodium
C	0030041	biological_process	actin filament polymerization
C	0030175	cellular_component	filopodium
C	0030240	biological_process	skeletal muscle thin filament assembly
C	0031013	molecular_function	troponin I binding
C	0031432	molecular_function	titin binding
C	0031941	cellular_component	filamentous actin
C	0032036	molecular_function	myosin heavy chain binding
C	0032432	cellular_component	actin filament bundle
C	0042802	molecular_function	identical protein binding
C	0044297	cellular_component	cell body
C	0048306	molecular_function	calcium-dependent protein binding
C	0048741	biological_process	skeletal muscle fiber development
C	0051017	biological_process	actin filament bundle assembly
C	0090131	biological_process	mesenchyme migration
C	0098723	cellular_component	skeletal muscle myofibril
C	0140660	molecular_function	cytoskeletal motor activator activity
D	0000166	molecular_function	nucleotide binding
D	0000287	molecular_function	magnesium ion binding
D	0001725	cellular_component	stress fiber
D	0003785	molecular_function	actin monomer binding
D	0005509	molecular_function	calcium ion binding
D	0005515	molecular_function	protein binding
D	0005523	molecular_function	tropomyosin binding
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0005856	cellular_component	cytoskeleton
D	0005865	cellular_component	striated muscle thin filament
D	0005884	cellular_component	actin filament
D	0010628	biological_process	positive regulation of gene expression
D	0016787	molecular_function	hydrolase activity
D	0019904	molecular_function	protein domain specific binding
D	0030027	cellular_component	lamellipodium
D	0030041	biological_process	actin filament polymerization
D	0030175	cellular_component	filopodium
D	0030240	biological_process	skeletal muscle thin filament assembly
D	0031013	molecular_function	troponin I binding
D	0031432	molecular_function	titin binding
D	0031941	cellular_component	filamentous actin
D	0032036	molecular_function	myosin heavy chain binding
D	0032432	cellular_component	actin filament bundle
D	0042802	molecular_function	identical protein binding
D	0044297	cellular_component	cell body
D	0048306	molecular_function	calcium-dependent protein binding
D	0048741	biological_process	skeletal muscle fiber development
D	0051017	biological_process	actin filament bundle assembly
D	0090131	biological_process	mesenchyme migration
D	0098723	cellular_component	skeletal muscle myofibril
D	0140660	molecular_function	cytoskeletal motor activator activity
E	0000166	molecular_function	nucleotide binding
E	0000287	molecular_function	magnesium ion binding
E	0001725	cellular_component	stress fiber
E	0003785	molecular_function	actin monomer binding
E	0005509	molecular_function	calcium ion binding
E	0005515	molecular_function	protein binding
E	0005523	molecular_function	tropomyosin binding
E	0005524	molecular_function	ATP binding
E	0005737	cellular_component	cytoplasm
E	0005856	cellular_component	cytoskeleton
E	0005865	cellular_component	striated muscle thin filament
E	0005884	cellular_component	actin filament
E	0010628	biological_process	positive regulation of gene expression
E	0016787	molecular_function	hydrolase activity
E	0019904	molecular_function	protein domain specific binding
E	0030027	cellular_component	lamellipodium
E	0030041	biological_process	actin filament polymerization
E	0030175	cellular_component	filopodium
E	0030240	biological_process	skeletal muscle thin filament assembly
E	0031013	molecular_function	troponin I binding
E	0031432	molecular_function	titin binding
E	0031941	cellular_component	filamentous actin
E	0032036	molecular_function	myosin heavy chain binding
E	0032432	cellular_component	actin filament bundle
E	0042802	molecular_function	identical protein binding
E	0044297	cellular_component	cell body
E	0048306	molecular_function	calcium-dependent protein binding
E	0048741	biological_process	skeletal muscle fiber development
E	0051017	biological_process	actin filament bundle assembly
E	0090131	biological_process	mesenchyme migration
E	0098723	cellular_component	skeletal muscle myofibril
E	0140660	molecular_function	cytoskeletal motor activator activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	16
Details	binding site for residue ADP A 376

Chain	Residue
A	GLY13
A	GLU214
A	GLY301
A	GLY302
A	MET305
A	TYR306
A	LYS336
A	MG377
A	SER14
A	GLY15
A	LEU16
A	LYS18
A	GLY156
A	ASP157
A	GLY158
A	LYS213

site_id	AC2
Number of Residues	3
Details	binding site for residue MG A 377

Chain	Residue
A	GLN137
A	ASP154
A	ADP376

site_id	AC3
Number of Residues	16
Details	binding site for residue ADP B 376

Chain	Residue
B	GLY13
B	SER14
B	GLY15
B	LEU16
B	LYS18
B	GLY156
B	ASP157
B	GLY158
B	LYS213
B	GLU214
B	GLY301
B	GLY302
B	MET305
B	TYR306
B	LYS336
B	MG377

site_id	AC4
Number of Residues	3
Details	binding site for residue MG B 377

Chain	Residue
B	GLN137
B	ASP154
B	ADP376

site_id	AC5
Number of Residues	16
Details	binding site for residue ADP C 376

Chain	Residue
C	GLY13
C	SER14
C	GLY15
C	LEU16
C	LYS18
C	GLY156
C	ASP157
C	GLY158
C	LYS213
C	GLU214
C	GLY301
C	GLY302
C	MET305
C	TYR306
C	LYS336
C	MG377

site_id	AC6
Number of Residues	3
Details	binding site for residue MG C 377

Chain	Residue
C	GLN137
C	ASP154
C	ADP376

site_id	AC7
Number of Residues	16
Details	binding site for residue ADP D 376

Chain	Residue
D	GLY13
D	SER14
D	GLY15
D	LEU16
D	LYS18
D	GLY156
D	ASP157
D	GLY158
D	LYS213
D	GLU214
D	GLY301
D	GLY302
D	MET305
D	TYR306
D	LYS336
D	MG377

site_id	AC8
Number of Residues	3
Details	binding site for residue MG D 377

Chain	Residue
D	GLN137
D	ASP154
D	ADP376

site_id	AC9
Number of Residues	16
Details	binding site for residue ADP E 376

Chain	Residue
E	GLY13
E	SER14
E	GLY15
E	LEU16
E	LYS18
E	GLY156
E	ASP157
E	GLY158
E	LYS213
E	GLU214
E	GLY301
E	GLY302
E	MET305
E	TYR306
E	LYS336
E	MG377

site_id	AD1
Number of Residues	3
Details	binding site for residue MG E 377

Chain	Residue
E	GLN137
E	ASP154
E	ADP376

site_id	AD2
Number of Residues	7
Details	binding site for Di-peptide TRP F 1 and EEP F 2

Chain	Residue
F	CYS5
F	HYP6
F	ALA7
A	ILE75
A	PRO112
F	ALA3
F	DTH4

site_id	AD3
Number of Residues	2
Details	binding site for Di-peptide EEP F 2 and ALA F 3

Chain	Residue
F	TRP1
F	DTH4

site_id	AD4
Number of Residues	4
Details	binding site for Di-peptide ALA F 3 and DTH F 4

Chain	Residue
B	ARG290
F	TRP1
F	EEP2
F	CYS5

site_id	AD5
Number of Residues	5
Details	binding site for Di-peptide DTH F 4 and CYS F 5

Chain	Residue
B	ARG290
F	TRP1
F	ALA3
F	HYP6
F	ALA7

site_id	AD6
Number of Residues	4
Details	binding site for Di-peptide CYS F 5 and HYP F 6

Chain	Residue
A	GLU72
F	TRP1
F	DTH4
F	ALA7

site_id	AD7
Number of Residues	3
Details	binding site for Di-peptide HYP F 6 and ALA F 7

Chain	Residue
A	GLU72
F	TRP1
F	CYS5

site_id	AD8
Number of Residues	11
Details	binding site for Di-peptide TRP G 1 and EEP G 2

Chain	Residue
A	GLY197
A	TYR198
A	SER199
A	GLN246
B	ILE75
B	PRO112
G	ALA3
G	DTH4
G	CYS5
G	HYP6
G	ALA7

site_id	AD9
Number of Residues	6
Details	binding site for Di-peptide EEP G 2 and ALA G 3

Chain	Residue
A	GLY197
A	TYR198
A	SER199
A	GLN246
G	TRP1
G	DTH4

site_id	AE1
Number of Residues	8
Details	binding site for Di-peptide ALA G 3 and DTH G 4

Chain	Residue
A	TYR198
A	SER199
A	GLU205
A	GLN246
C	ARG290
G	TRP1
G	EEP2
G	CYS5

site_id	AE2
Number of Residues	7
Details	binding site for Di-peptide DTH G 4 and CYS G 5

Chain	Residue
A	SER199
A	GLU205
C	ARG290
G	TRP1
G	ALA3
G	HYP6
G	ALA7

site_id	AE3
Number of Residues	4
Details	binding site for Di-peptide CYS G 5 and HYP G 6

Chain	Residue
B	GLU72
G	TRP1
G	DTH4
G	ALA7

site_id	AE4
Number of Residues	3
Details	binding site for Di-peptide HYP G 6 and ALA G 7

Chain	Residue
B	GLU72
G	TRP1
G	CYS5

site_id	AE5
Number of Residues	11
Details	binding site for Di-peptide TRP H 1 and EEP H 2

Chain	Residue
B	GLY197
B	TYR198
B	SER199
B	GLN246
C	ILE75
C	PRO112
H	ALA3
H	DTH4
H	CYS5
H	HYP6
H	ALA7

site_id	AE6
Number of Residues	6
Details	binding site for Di-peptide EEP H 2 and ALA H 3

Chain	Residue
B	GLY197
B	TYR198
B	SER199
B	GLN246
H	TRP1
H	DTH4

site_id	AE7
Number of Residues	8
Details	binding site for Di-peptide ALA H 3 and DTH H 4

Chain	Residue
B	TYR198
B	SER199
B	GLU205
B	GLN246
D	ARG290
H	TRP1
H	EEP2
H	CYS5

site_id	AE8
Number of Residues	7
Details	binding site for Di-peptide DTH H 4 and CYS H 5

Chain	Residue
B	SER199
B	GLU205
D	ARG290
H	TRP1
H	ALA3
H	HYP6
H	ALA7

site_id	AE9
Number of Residues	4
Details	binding site for Di-peptide CYS H 5 and HYP H 6

Chain	Residue
C	GLU72
H	TRP1
H	DTH4
H	ALA7

site_id	AF1
Number of Residues	3
Details	binding site for Di-peptide HYP H 6 and ALA H 7

Chain	Residue
C	GLU72
H	TRP1
H	CYS5

site_id	AF2
Number of Residues	11
Details	binding site for Di-peptide TRP I 1 and EEP I 2

Chain	Residue
C	GLY197
C	TYR198
C	SER199
C	GLN246
D	ILE75
D	PRO112
I	ALA3
I	DTH4
I	CYS5
I	HYP6
I	ALA7

site_id	AF3
Number of Residues	6
Details	binding site for Di-peptide EEP I 2 and ALA I 3

Chain	Residue
C	GLY197
C	TYR198
C	SER199
C	GLN246
I	TRP1
I	DTH4

site_id	AF4
Number of Residues	8
Details	binding site for Di-peptide ALA I 3 and DTH I 4

Chain	Residue
C	TYR198
C	SER199
C	GLU205
C	GLN246
E	ARG290
I	TRP1
I	EEP2
I	CYS5

site_id	AF5
Number of Residues	7
Details	binding site for Di-peptide DTH I 4 and CYS I 5

Chain	Residue
C	SER199
C	GLU205
E	ARG290
I	TRP1
I	ALA3
I	HYP6
I	ALA7

site_id	AF6
Number of Residues	4
Details	binding site for Di-peptide CYS I 5 and HYP I 6

Chain	Residue
D	GLU72
I	TRP1
I	DTH4
I	ALA7

site_id	AF7
Number of Residues	3
Details	binding site for Di-peptide HYP I 6 and ALA I 7

Chain	Residue
D	GLU72
I	TRP1
I	CYS5

site_id	AF8
Number of Residues	11
Details	binding site for Di-peptide TRP J 1 and EEP J 2

Chain	Residue
D	GLY197
D	TYR198
D	SER199
D	GLN246
E	ILE75
E	PRO112
J	ALA3
J	DTH4
J	CYS5
J	HYP6
J	ALA7

site_id	AF9
Number of Residues	6
Details	binding site for Di-peptide EEP J 2 and ALA J 3

Chain	Residue
D	GLY197
D	TYR198
D	SER199
D	GLN246
J	TRP1
J	DTH4

site_id	AG1
Number of Residues	7
Details	binding site for Di-peptide ALA J 3 and DTH J 4

Chain	Residue
D	TYR198
D	SER199
D	GLU205
D	GLN246
J	TRP1
J	EEP2
J	CYS5

site_id	AG2
Number of Residues	6
Details	binding site for Di-peptide DTH J 4 and CYS J 5

Chain	Residue
D	SER199
D	GLU205
J	TRP1
J	ALA3
J	HYP6
J	ALA7

site_id	AG3
Number of Residues	4
Details	binding site for Di-peptide CYS J 5 and HYP J 6

Chain	Residue
E	GLU72
J	TRP1
J	DTH4
J	ALA7

site_id	AG4
Number of Residues	3
Details	binding site for Di-peptide HYP J 6 and ALA J 7

Chain	Residue
E	GLU72
J	TRP1
J	CYS5

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

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

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	65
Details	Region: {"description":"Interaction with alpha-actinin","evidences":[{"source":"PubMed","id":"8449927","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	5
Details	Modified residue: {"description":"N6-malonyllysine","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	5
Details	Modified residue: {"description":"Tele-methylhistidine","evidences":[{"source":"PubMed","id":"1150665","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16905096","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"213279","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2395459","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"499690","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1ATN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NWK","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	5
Details	Modified residue: {"description":"N6-methyllysine","evidences":[{"source":"UniProtKB","id":"P68133","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	5
Details	Modified residue: {"description":"ADP-ribosylarginine; by SpvB","evidences":[{"source":"PubMed","id":"16905096","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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