Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6D8C

Cryo-EM structure of FLNaABD E254K bound to phalloidin-stabilized F-actin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0030036	biological_process	actin cytoskeleton organization
A	0051015	molecular_function	actin filament binding
B	0030036	biological_process	actin cytoskeleton organization
B	0051015	molecular_function	actin filament binding
C	0030036	biological_process	actin cytoskeleton organization
C	0051015	molecular_function	actin filament binding
D	0030036	biological_process	actin cytoskeleton organization
D	0051015	molecular_function	actin filament binding
E	0030036	biological_process	actin cytoskeleton organization
E	0051015	molecular_function	actin filament binding
H	0000166	molecular_function	nucleotide binding
H	0001725	cellular_component	stress fiber
H	0005515	molecular_function	protein binding
H	0005524	molecular_function	ATP binding
H	0005737	cellular_component	cytoplasm
H	0005856	cellular_component	cytoskeleton
H	0005865	cellular_component	striated muscle thin filament
H	0005884	cellular_component	actin filament
H	0015629	cellular_component	actin cytoskeleton
H	0016787	molecular_function	hydrolase activity
H	0030240	biological_process	skeletal muscle thin filament assembly
H	0048741	biological_process	skeletal muscle fiber development
J	0000166	molecular_function	nucleotide binding
J	0001725	cellular_component	stress fiber
J	0005515	molecular_function	protein binding
J	0005524	molecular_function	ATP binding
J	0005737	cellular_component	cytoplasm
J	0005856	cellular_component	cytoskeleton
J	0005865	cellular_component	striated muscle thin filament
J	0005884	cellular_component	actin filament
J	0015629	cellular_component	actin cytoskeleton
J	0016787	molecular_function	hydrolase activity
J	0030240	biological_process	skeletal muscle thin filament assembly
J	0048741	biological_process	skeletal muscle fiber development
K	0000166	molecular_function	nucleotide binding
K	0001725	cellular_component	stress fiber
K	0005515	molecular_function	protein binding
K	0005524	molecular_function	ATP binding
K	0005737	cellular_component	cytoplasm
K	0005856	cellular_component	cytoskeleton
K	0005865	cellular_component	striated muscle thin filament
K	0005884	cellular_component	actin filament
K	0015629	cellular_component	actin cytoskeleton
K	0016787	molecular_function	hydrolase activity
K	0030240	biological_process	skeletal muscle thin filament assembly
K	0048741	biological_process	skeletal muscle fiber development
L	0000166	molecular_function	nucleotide binding
L	0001725	cellular_component	stress fiber
L	0005515	molecular_function	protein binding
L	0005524	molecular_function	ATP binding
L	0005737	cellular_component	cytoplasm
L	0005856	cellular_component	cytoskeleton
L	0005865	cellular_component	striated muscle thin filament
L	0005884	cellular_component	actin filament
L	0015629	cellular_component	actin cytoskeleton
L	0016787	molecular_function	hydrolase activity
L	0030240	biological_process	skeletal muscle thin filament assembly
L	0048741	biological_process	skeletal muscle fiber development
M	0000166	molecular_function	nucleotide binding
M	0001725	cellular_component	stress fiber
M	0005515	molecular_function	protein binding
M	0005524	molecular_function	ATP binding
M	0005737	cellular_component	cytoplasm
M	0005856	cellular_component	cytoskeleton
M	0005865	cellular_component	striated muscle thin filament
M	0005884	cellular_component	actin filament
M	0015629	cellular_component	actin cytoskeleton
M	0016787	molecular_function	hydrolase activity
M	0030240	biological_process	skeletal muscle thin filament assembly
M	0048741	biological_process	skeletal muscle fiber development

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	binding site for residue ADP H 401

Chain	Residue
H	ASP11
H	LYS213
H	GLU214
H	GLY302
H	THR303
H	MET305
H	MG402
H	GLY13
H	SER14
H	GLY15
H	LEU16
H	LYS18
H	GLN137
H	GLY156
H	ASP157

site_id	AC2
Number of Residues	3
Details	binding site for residue MG H 402

Chain	Residue
H	GLN137
H	ASP154
H	ADP401

site_id	AC3
Number of Residues	15
Details	binding site for residue ADP J 401

Chain	Residue
J	ASP11
J	GLY13
J	SER14
J	GLY15
J	LEU16
J	LYS18
J	GLN137
J	GLY156
J	ASP157
J	LYS213
J	GLU214
J	GLY302
J	THR303
J	MET305
J	MG402

site_id	AC4
Number of Residues	3
Details	binding site for residue MG J 402

Chain	Residue
J	GLN137
J	ASP154
J	ADP401

site_id	AC5
Number of Residues	15
Details	binding site for residue ADP K 401

Chain	Residue
K	ASP11
K	GLY13
K	SER14
K	GLY15
K	LEU16
K	LYS18
K	GLN137
K	GLY156
K	ASP157
K	LYS213
K	GLU214
K	GLY302
K	THR303
K	MET305
K	MG402

site_id	AC6
Number of Residues	3
Details	binding site for residue MG K 402

Chain	Residue
K	GLN137
K	ASP154
K	ADP401

site_id	AC7
Number of Residues	15
Details	binding site for residue ADP L 401

Chain	Residue
L	ASP11
L	GLY13
L	SER14
L	GLY15
L	LEU16
L	LYS18
L	GLN137
L	GLY156
L	ASP157
L	LYS213
L	GLU214
L	GLY302
L	THR303
L	MET305
L	MG402

site_id	AC8
Number of Residues	3
Details	binding site for residue MG L 402

Chain	Residue
L	GLN137
L	ASP154
L	ADP401

site_id	AC9
Number of Residues	15
Details	binding site for residue ADP M 401

Chain	Residue
M	ASP11
M	GLY13
M	SER14
M	GLY15
M	LEU16
M	LYS18
M	GLN137
M	GLY156
M	ASP157
M	LYS213
M	GLU214
M	GLY302
M	THR303
M	MET305
M	MG402

site_id	AD1
Number of Residues	3
Details	binding site for residue MG M 402

Chain	Residue
M	GLN137
M	ASP154
M	ADP401

site_id	AD2
Number of Residues	11
Details	binding site for phalloidin chain N

Chain	Residue
K	ARG177
M	ILE287
H	GLY197
H	TYR198
H	SER199
H	PHE200
H	GLU205
H	GLN246
K	GLU72
K	ILE75
K	PRO112

site_id	AD3
Number of Residues	11
Details	binding site for phalloidin chain O

Chain	Residue
H	ILE287
J	GLY197
J	TYR198
J	SER199
J	PHE200
J	GLU205
J	GLN246
L	GLU72
L	ILE75
L	PRO112
L	ARG177

site_id	AD4
Number of Residues	11
Details	binding site for phalloidin chain P

Chain	Residue
H	GLU72
H	ILE75
H	PRO112
H	ARG177
K	ILE287
L	GLY197
L	TYR198
L	SER199
L	PHE200
L	GLU205
L	GLN246

Functional Information from PROSITE/UniProt

site_id	PS00019
Number of Residues	10
Details	ACTININ_1 Actinin-type actin-binding domain signature 1. QQnTFTRWCN

Chain	Residue	Details
D	GLN45-ASN54

site_id	PS00020
Number of Residues	25
Details	ACTININ_2 Actinin-type actin-binding domain signature 2. LvSIDSkAIvDgnlkLiLGLIWtLI

Chain	Residue	Details
D	LEU121-ILE145

site_id	PS00406
Number of Residues	11
Details	ACTINS_1 Actins signature 1. YVGDEAQs.KRG

Chain	Residue	Details
H	TYR53-GLY63

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

Chain	Residue	Details
H	TRP356-GLU364

site_id	PS01132
Number of Residues	13
Details	ACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR

Chain	Residue	Details
H	LEU104-ARG116

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	CROSSLNK: 2'-cysteinyl-6'-hydroxytryptophan sulfoxide (Trp-Cys) => ECO:0000250\|UniProtKB:P85421

Chain	Residue	Details
N	TRP3
N	CYS7
O	TRP3
O	CYS7
P	TRP3
P	CYS7

site_id	SWS_FT_FI2
Number of Residues	10
Details	MOD_RES: Methionine (R)-sulfoxide => ECO:0000250\|UniProtKB:P68134

Chain	Residue	Details
H	MET44
M	MET47
H	MET47
J	MET44
J	MET47
K	MET44
K	MET47
L	MET44
L	MET47
M	MET44

site_id	SWS_FT_FI3
Number of Residues	5
Details	MOD_RES: Tele-methylhistidine => ECO:0000269\|PubMed:12356759, ECO:0007744\|PDB:1MDU

Chain	Residue	Details
H	HIS73
B	LYS43
B	LYS135
C	LYS42
C	LYS43
C	LYS135
E	LYS42
E	LYS43
J	HIS73
E	LYS135
K	HIS73
L	HIS73
M	HIS73
A	LYS43
A	LYS135
B	LYS42

site_id	SWS_FT_FI4
Number of Residues	5
Details	MOD_RES: N6-methyllysine => ECO:0000250\|UniProtKB:P68133

Chain	Residue	Details
H	LYS84
J	LYS84
K	LYS84
L	LYS84
M	LYS84

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