4A7H

Structure of the Actin-Tropomyosin-Myosin Complex (rigor ATM 2)

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
C	0003774	molecular_function	cytoskeletal motor activity
C	0005524	molecular_function	ATP binding
C	0016459	cellular_component	myosin complex
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
I	0003774	molecular_function	cytoskeletal motor activity
I	0005524	molecular_function	ATP binding
I	0016459	cellular_component	myosin complex
J	0003774	molecular_function	cytoskeletal motor activity
J	0005524	molecular_function	ATP binding
J	0016459	cellular_component	myosin complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE ADP A 376

Chain	Residue
A	LEU16
A	TYR306
A	LYS336
A	CA377
A	LYS18
A	GLY156
A	ASP157
A	GLY158
A	LYS213
A	GLU214
A	GLY302
A	MET305

---

site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CA A 377

Chain	Residue
A	GLY156
A	ADP376

---

site_id	AC3
Number of Residues	12
Details	BINDING SITE FOR RESIDUE ADP D 376

Chain	Residue
D	LEU16
D	LYS18
D	GLY156
D	ASP157
D	GLY158
D	LYS213
D	GLU214
D	GLY302
D	MET305
D	TYR306
D	LYS336
D	CA377

---

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CA D 377

Chain	Residue
D	GLY156
D	ADP376

---

site_id	AC5
Number of Residues	12
Details	BINDING SITE FOR RESIDUE ADP E 376

Chain	Residue
E	LEU16
E	LYS18
E	GLY156
E	ASP157
E	GLY158
E	LYS213
E	GLU214
E	GLY302
E	MET305
E	TYR306
E	LYS336
E	CA377

---

site_id	AC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CA E 377

Chain	Residue
E	GLY156
E	ADP376

---

site_id	AC7
Number of Residues	12
Details	BINDING SITE FOR RESIDUE ADP F 376

Chain	Residue
F	LEU16
F	LYS18
F	GLY156
F	ASP157
F	GLY158
F	LYS213
F	GLU214
F	GLY302
F	MET305
F	TYR306
F	LYS336
F	CA377

---

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CA F 377

Chain	Residue
F	GLY156
F	ADP376

---

site_id	AC9
Number of Residues	12
Details	BINDING SITE FOR RESIDUE ADP G 376

Chain	Residue
G	LEU16
G	LYS18
G	GLY156
G	ASP157
G	GLY158
G	LYS213
G	GLU214
G	GLY302
G	MET305
G	TYR306
G	LYS336
G	CA377

---

site_id	BC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CA G 377

Chain	Residue
G	GLY156
G	ADP376

---

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	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

---

site_id	SWS_FT_FI8
Number of Residues	109
Details	Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P09493","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P58771","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	222
Details	Region: {"description":"Actin-binding"}

Chain

Residue

Details

---

site_id	SWS_FT_FI12
Number of Residues	27
Details	Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI13
Number of Residues	21
Details	Binding site: {}

Chain

Residue

Details

---