Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6U96

Actin phalloidin at BeFx state

Functional Information from GO Data

Chain	GOid	namespace	contents
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	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	0016887	molecular_function	ATP hydrolysis 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	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	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	0016887	molecular_function	ATP hydrolysis 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	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	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	0016887	molecular_function	ATP hydrolysis 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	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	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	0016887	molecular_function	ATP hydrolysis 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	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	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	0016887	molecular_function	ATP hydrolysis 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	8
Details	binding site for residue ADP A 801

Chain	Residue
A	GLY13
A	SER14
A	GLY156
A	ASP157
A	LYS213
A	GLU214
A	GLY302
A	TYR306

site_id	AC2
Number of Residues	8
Details	binding site for residue ADP B 801

Chain	Residue
B	SER14
B	GLY156
B	ASP157
B	LYS213
B	GLU214
B	GLY302
B	TYR306
B	GLY13

site_id	AC3
Number of Residues	8
Details	binding site for residue ADP C 401

Chain	Residue
C	GLY13
C	SER14
C	GLY156
C	ASP157
C	LYS213
C	GLU214
C	GLY302
C	TYR306

site_id	AC4
Number of Residues	8
Details	binding site for residue ADP D 801

Chain	Residue
D	GLY13
D	SER14
D	GLY156
D	ASP157
D	LYS213
D	GLU214
D	GLY302
D	TYR306

site_id	AC5
Number of Residues	8
Details	binding site for residue ADP E 401

Chain	Residue
E	GLY13
E	SER14
E	GLY156
E	ASP157
E	LYS213
E	GLU214
E	GLY302
E	TYR306

site_id	AC6
Number of Residues	6
Details	binding site for Di-peptide EEP F 1 and TRP F 7

Chain	Residue
A	GLY197
B	PRO112
F	ALA2
F	CYS4
F	HYP5
F	ALA6

site_id	AC7
Number of Residues	3
Details	binding site for Di-peptide EEP F 1 and ALA F 2

Chain	Residue
A	GLY197
F	ALO3
F	TRP7

site_id	AC8
Number of Residues	3
Details	binding site for Di-peptide ALA F 2 and ALO F 3

Chain	Residue
A	SER199
F	EEP1
F	CYS4

site_id	AC9
Number of Residues	5
Details	binding site for Di-peptide ALO F 3 and CYS F 4

Chain	Residue
A	SER199
F	ALA2
F	HYP5
F	ALA6
F	TRP7

site_id	AD1
Number of Residues	3
Details	binding site for Di-peptide CYS F 4 and HYP F 5

Chain	Residue
F	ALO3
F	ALA6
F	TRP7

site_id	AD2
Number of Residues	3
Details	binding site for Di-peptide HYP F 5 and ALA F 6

Chain	Residue
B	GLU72
F	CYS4
F	TRP7

site_id	AD3
Number of Residues	6
Details	binding site for Di-peptide EEP G 1 and TRP G 7

Chain	Residue
B	GLY197
D	PRO112
G	ALA2
G	CYS4
G	HYP5
G	ALA6

site_id	AD4
Number of Residues	4
Details	binding site for Di-peptide EEP G 1 and ALA G 2

Chain	Residue
B	GLY197
B	TYR198
G	ALO3
G	TRP7

site_id	AD5
Number of Residues	5
Details	binding site for Di-peptide ALA G 2 and ALO G 3

Chain	Residue
B	GLY197
B	TYR198
B	SER199
G	EEP1
G	CYS4

site_id	AD6
Number of Residues	5
Details	binding site for Di-peptide ALO G 3 and CYS G 4

Chain	Residue
B	SER199
G	ALA2
G	HYP5
G	ALA6
G	TRP7

site_id	AD7
Number of Residues	3
Details	binding site for Di-peptide CYS G 4 and HYP G 5

Chain	Residue
G	ALO3
G	ALA6
G	TRP7

site_id	AD8
Number of Residues	3
Details	binding site for Di-peptide HYP G 5 and ALA G 6

Chain	Residue
D	GLU72
G	CYS4
G	TRP7

site_id	AD9
Number of Residues	6
Details	binding site for Di-peptide EEP H 1 and TRP H 7

Chain	Residue
A	PRO112
C	GLY197
H	ALA2
H	CYS4
H	HYP5
H	ALA6

site_id	AE1
Number of Residues	3
Details	binding site for Di-peptide EEP H 1 and ALA H 2

Chain	Residue
C	GLY197
H	ALO3
H	TRP7

site_id	AE2
Number of Residues	3
Details	binding site for Di-peptide ALA H 2 and ALO H 3

Chain	Residue
H	EEP1
H	CYS4
C	SER199

site_id	AE3
Number of Residues	5
Details	binding site for Di-peptide ALO H 3 and CYS H 4

Chain	Residue
C	SER199
H	ALA2
H	HYP5
H	ALA6
H	TRP7

site_id	AE4
Number of Residues	3
Details	binding site for Di-peptide CYS H 4 and HYP H 5

Chain	Residue
H	ALO3
H	ALA6
H	TRP7

site_id	AE5
Number of Residues	3
Details	binding site for Di-peptide HYP H 5 and ALA H 6

Chain	Residue
A	GLU72
H	CYS4
H	TRP7

site_id	AE6
Number of Residues	3
Details	binding site for Di-peptide EEP I 1 and ALA I 2

Chain	Residue
E	GLY197
I	ALO3
I	TRP7

site_id	AE7
Number of Residues	6
Details	binding site for Di-peptide EEP I 1 and TRP I 7

Chain	Residue
C	PRO112
E	GLY197
I	ALA2
I	CYS4
I	HYP5
I	ALA6

site_id	AE8
Number of Residues	3
Details	binding site for Di-peptide ALA I 2 and ALO I 3

Chain	Residue
E	SER199
I	EEP1
I	CYS4

site_id	AE9
Number of Residues	5
Details	binding site for Di-peptide ALO I 3 and CYS I 4

Chain	Residue
E	SER199
I	ALA2
I	HYP5
I	ALA6
I	TRP7

site_id	AF1
Number of Residues	3
Details	binding site for Di-peptide CYS I 4 and HYP I 5

Chain	Residue
I	ALO3
I	ALA6
I	TRP7

site_id	AF2
Number of Residues	3
Details	binding site for Di-peptide HYP I 5 and ALA I 6

Chain	Residue
C	GLU72
I	CYS4
I	TRP7

site_id	AF3
Number of Residues	2
Details	binding site for Di-peptide EEP J 1 and ALA J 2

Chain	Residue
J	ALO3
J	TRP7

site_id	AF4
Number of Residues	5
Details	binding site for Di-peptide EEP J 1 and TRP J 7

Chain	Residue
E	PRO112
J	ALA2
J	CYS4
J	HYP5
J	ALA6

site_id	AF5
Number of Residues	2
Details	binding site for Di-peptide ALA J 2 and ALO J 3

Chain	Residue
J	EEP1
J	CYS4

site_id	AF6
Number of Residues	4
Details	binding site for Di-peptide ALO J 3 and CYS J 4

Chain	Residue
J	ALA2
J	HYP5
J	ALA6
J	TRP7

site_id	AF7
Number of Residues	3
Details	binding site for Di-peptide CYS J 4 and HYP J 5

Chain	Residue
J	ALO3
J	ALA6
J	TRP7

site_id	AF8
Number of Residues	3
Details	binding site for Di-peptide HYP J 5 and ALA J 6

Chain	Residue
E	GLU72
J	CYS4
J	TRP7

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	125
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	10
Details	Modified residue: {"description":"Methionine (R)-sulfoxide","evidences":[{"source":"UniProtKB","id":"P68134","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	5
Details	Modified residue: {"description":"N6-malonyllysine","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
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_FI5
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_FI6
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)