5YU8

Cofilin decorated actin filament

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001725	cellular_component	stress fiber
A	0005515	molecular_function	protein 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	0016787	molecular_function	hydrolase activity
A	0030240	biological_process	skeletal muscle thin filament assembly
A	0048741	biological_process	skeletal muscle fiber development
B	0001725	cellular_component	stress fiber
B	0005515	molecular_function	protein 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	0016787	molecular_function	hydrolase activity
B	0030240	biological_process	skeletal muscle thin filament assembly
B	0048741	biological_process	skeletal muscle fiber development
C	0001725	cellular_component	stress fiber
C	0005515	molecular_function	protein 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	0016787	molecular_function	hydrolase activity
C	0030240	biological_process	skeletal muscle thin filament assembly
C	0048741	biological_process	skeletal muscle fiber development
D	0001725	cellular_component	stress fiber
D	0005515	molecular_function	protein 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	0016787	molecular_function	hydrolase activity
D	0030240	biological_process	skeletal muscle thin filament assembly
D	0048741	biological_process	skeletal muscle fiber development
E	0001725	cellular_component	stress fiber
E	0005515	molecular_function	protein 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	0016787	molecular_function	hydrolase activity
E	0030240	biological_process	skeletal muscle thin filament assembly
E	0048741	biological_process	skeletal muscle fiber development
H	0003779	molecular_function	actin binding
H	0005634	cellular_component	nucleus
H	0005737	cellular_component	cytoplasm
H	0005856	cellular_component	cytoskeleton
H	0015629	cellular_component	actin cytoskeleton
H	0016363	cellular_component	nuclear matrix
H	0030042	biological_process	actin filament depolymerization
H	0030043	biological_process	actin filament fragmentation
H	0051014	biological_process	actin filament severing
H	0051015	molecular_function	actin filament binding
I	0003779	molecular_function	actin binding
I	0005634	cellular_component	nucleus
I	0005737	cellular_component	cytoplasm
I	0005856	cellular_component	cytoskeleton
I	0015629	cellular_component	actin cytoskeleton
I	0016363	cellular_component	nuclear matrix
I	0030042	biological_process	actin filament depolymerization
I	0030043	biological_process	actin filament fragmentation
I	0051014	biological_process	actin filament severing
I	0051015	molecular_function	actin filament binding
J	0003779	molecular_function	actin binding
J	0005634	cellular_component	nucleus
J	0005737	cellular_component	cytoplasm
J	0005856	cellular_component	cytoskeleton
J	0015629	cellular_component	actin cytoskeleton
J	0016363	cellular_component	nuclear matrix
J	0030042	biological_process	actin filament depolymerization
J	0030043	biological_process	actin filament fragmentation
J	0051014	biological_process	actin filament severing
J	0051015	molecular_function	actin filament binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	1
Details	binding site for residue MG A 401

Chain	Residue
A	ADP402

---

site_id	AC2
Number of Residues	17
Details	binding site for residue ADP A 402

Chain	Residue
A	LYS213
A	GLU214
A	GLY301
A	GLY302
A	THR303
A	MET305
A	TYR306
A	LYS336
A	MG401
A	GLY13
A	SER14
A	GLY15
A	LEU16
A	LYS18
A	GLY156
A	ASP157
A	ARG210

---

site_id	AC3
Number of Residues	1
Details	binding site for residue MG B 401

Chain	Residue
B	ADP402

---

site_id	AC4
Number of Residues	17
Details	binding site for residue ADP B 402

Chain	Residue
B	GLY13
B	SER14
B	GLY15
B	LEU16
B	LYS18
B	GLY156
B	ASP157
B	ARG210
B	LYS213
B	GLU214
B	GLY301
B	GLY302
B	THR303
B	MET305
B	TYR306
B	LYS336
B	MG401

---

site_id	AC5
Number of Residues	1
Details	binding site for residue MG C 401

Chain	Residue
C	ADP402

---

site_id	AC6
Number of Residues	17
Details	binding site for residue ADP C 402

Chain	Residue
C	GLY13
C	SER14
C	GLY15
C	LEU16
C	LYS18
C	GLY156
C	ASP157
C	ARG210
C	LYS213
C	GLU214
C	GLY301
C	GLY302
C	THR303
C	MET305
C	TYR306
C	LYS336
C	MG401

---

site_id	AC7
Number of Residues	1
Details	binding site for residue MG D 401

Chain	Residue
D	ADP402

---

site_id	AC8
Number of Residues	17
Details	binding site for residue ADP D 402

Chain	Residue
D	GLY13
D	SER14
D	GLY15
D	LEU16
D	LYS18
D	GLY156
D	ASP157
D	ARG210
D	LYS213
D	GLU214
D	GLY301
D	GLY302
D	THR303
D	MET305
D	TYR306
D	LYS336
D	MG401

---

site_id	AC9
Number of Residues	1
Details	binding site for residue MG E 401

Chain	Residue
E	ADP402

---

site_id	AD1
Number of Residues	17
Details	binding site for residue ADP E 402

Chain	Residue
E	GLY13
E	SER14
E	GLY15
E	LEU16
E	LYS18
E	GLY156
E	ASP157
E	ARG210
E	LYS213
E	GLU214
E	GLY301
E	GLY302
E	THR303
E	MET305
E	TYR306
E	LYS336
E	MG401

---

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	3
Details	MOD_RES: Phosphoserine => ECO:0000250

Chain	Residue	Details
H	SER24
I	SER24
J	SER24
D	ASP1
E	ASP1

---

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

Chain	Residue	Details
A	MET44
A	MET47
B	MET44
B	MET47
C	MET44
C	MET47
D	MET44
D	MET47
E	MET44
E	MET47

---

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
A	HIC73
B	HIC73
C	HIC73
D	HIC73
E	HIC73

---

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

Chain	Residue	Details
A	LYS84
B	LYS84
C	LYS84
D	LYS84
E	LYS84

---