3J8I

Near-Atomic Resolution for One State of F-Actin

Functional Information from GO Data

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	BINDING SITE FOR RESIDUE ADP D 401

Chain	Residue
D	ASP11
D	ARG210
D	LYS213
D	GLU214
D	GLY302
D	THR303
D	MET305
D	TYR306
D	MG402
D	GLY13
D	SER14
D	GLY15
D	LEU16
D	GLY156
D	ASP157
D	GLY182
D	ARG183

---

site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG D 402

Chain	Residue
D	ASP154
D	ADP401

---

site_id	AC3
Number of Residues	17
Details	BINDING SITE FOR RESIDUE ADP E 401

Chain	Residue
E	ASP11
E	GLY13
E	SER14
E	GLY15
E	LEU16
E	GLY156
E	ASP157
E	GLY182
E	ARG183
E	ARG210
E	LYS213
E	GLU214
E	GLY302
E	THR303
E	MET305
E	TYR306
E	MG402

---

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG E 402

Chain	Residue
E	ASP154
E	ADP401

---

site_id	AC5
Number of Residues	17
Details	BINDING SITE FOR RESIDUE ADP F 401

Chain	Residue
F	ASP11
F	GLY13
F	SER14
F	GLY15
F	LEU16
F	GLY156
F	ASP157
F	GLY182
F	ARG183
F	ARG210
F	LYS213
F	GLU214
F	GLY302
F	THR303
F	MET305
F	TYR306
F	MG402

---

site_id	AC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG F 402

Chain	Residue
F	ASP154
F	ADP401

---

site_id	AC7
Number of Residues	17
Details	BINDING SITE FOR RESIDUE ADP G 401

Chain	Residue
G	ASP11
G	GLY13
G	SER14
G	GLY15
G	LEU16
G	GLY156
G	ASP157
G	GLY182
G	ARG183
G	ARG210
G	LYS213
G	GLU214
G	GLY302
G	THR303
G	MET305
G	TYR306
G	MG402

---

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG G 402

Chain	Residue
G	ASP154
G	ADP401

---

site_id	AC9
Number of Residues	17
Details	BINDING SITE FOR RESIDUE ADP H 401

Chain	Residue
H	ASP11
H	GLY13
H	SER14
H	GLY15
H	LEU16
H	GLY156
H	ASP157
H	GLY182
H	ARG183
H	ARG210
H	LYS213
H	GLU214
H	GLY302
H	THR303
H	MET305
H	TYR306
H	MG402

---

site_id	BC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG H 402

Chain	Residue
H	ASP154
H	ADP401

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
D	TYR53-GLY63

---

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

Chain	Residue	Details
D	TRP356-GLU364

---

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

Chain	Residue	Details
D	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	5
Details	Modified residue: {"description":"N-acetylaspartate; in Actin, alpha skeletal muscle","evidences":[{"source":"PubMed","id":"1150665","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
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_FI4
Number of Residues	5
Details	Modified residue: {"description":"N6-malonyllysine","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
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_FI6
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_FI7
Number of Residues	5
Details	Modified residue: {"description":"ADP-ribosylarginine; by SpvB","evidences":[{"source":"PubMed","id":"16905096","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---