Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7PME

Cryo-EM structure of the actomyosin-V complex in the post-rigor transition state (AppNHp, central 3er/2er)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003774	molecular_function	cytoskeletal motor activity
A	0005524	molecular_function	ATP binding
A	0016459	cellular_component	myosin complex
B	0005509	molecular_function	calcium ion binding
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	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	0010628	biological_process	positive regulation of gene expression
C	0016787	molecular_function	hydrolase 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	0003774	molecular_function	cytoskeletal motor activity
D	0005524	molecular_function	ATP binding
D	0016459	cellular_component	myosin complex
E	0005509	molecular_function	calcium ion 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	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

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
C	TYR53-GLY63

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

Chain	Residue	Details
C	TRP356-GLU364

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

Chain	Residue	Details
C	LEU104-ARG116

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	MOD_RES: N-acetylcysteine; in intermediate form => ECO:0000250\|UniProtKB:P62737

Chain	Residue	Details
F	CYS0
G	CYS0
C	CYS0

site_id	SWS_FT_FI2
Number of Residues	3
Details	MOD_RES: N-acetylaspartate; in Actin, alpha skeletal muscle => ECO:0000269\|PubMed:1150665

Chain	Residue	Details
F	ASP1
G	ASP1
C	ASP1

site_id	SWS_FT_FI3
Number of Residues	6
Details	MOD_RES: Methionine (R)-sulfoxide => ECO:0000250\|UniProtKB:P68134

Chain	Residue	Details
F	MET44
F	MET47
G	MET44
G	MET47
C	MET44
C	MET47

site_id	SWS_FT_FI4
Number of Residues	3
Details	MOD_RES: N6-malonyllysine => ECO:0000250

Chain	Residue	Details
F	LYS61
G	LYS61
C	LYS61

site_id	SWS_FT_FI5
Number of Residues	3
Details	MOD_RES: Tele-methylhistidine => ECO:0000269\|PubMed:1150665, ECO:0000269\|PubMed:16905096, ECO:0000269\|PubMed:213279, ECO:0000269\|PubMed:2395459, ECO:0000269\|PubMed:499690, ECO:0007744\|PDB:1ATN, ECO:0007744\|PDB:1NWK

Chain	Residue	Details
F	HIC73
G	HIC73
C	HIC73

site_id	SWS_FT_FI6
Number of Residues	3
Details	MOD_RES: N6-methyllysine => ECO:0000250\|UniProtKB:P68133

Chain	Residue	Details
F	LYS84
G	LYS84
C	LYS84

site_id	SWS_FT_FI7
Number of Residues	3
Details	MOD_RES: ADP-ribosylarginine; by SpvB => ECO:0000305\|PubMed:16905096

Chain	Residue	Details
F	ARG177
G	ARG177
C	ARG177

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