Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7ALN

Cryo-EM structure of the divergent actomyosin complex from Plasmodium falciparum Myosin A in the Rigor state

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005200	molecular_function	structural constituent of cytoskeleton
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005856	cellular_component	cytoskeleton
A	0005884	cellular_component	actin filament
A	0007010	biological_process	cytoskeleton organization
A	0009665	biological_process	plastid inheritance
A	0015629	cellular_component	actin cytoskeleton
A	0016787	molecular_function	hydrolase activity
A	0016887	molecular_function	ATP hydrolysis activity
A	0020014	biological_process	schizogony
A	0070360	biological_process	symbiont-mediated actin polymerization-dependent cell-to-cell migration in host
A	0085017	biological_process	entry into host cell by a symbiont-containing vacuole
B	0005200	molecular_function	structural constituent of cytoskeleton
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0005856	cellular_component	cytoskeleton
B	0005884	cellular_component	actin filament
B	0007010	biological_process	cytoskeleton organization
B	0009665	biological_process	plastid inheritance
B	0015629	cellular_component	actin cytoskeleton
B	0016787	molecular_function	hydrolase activity
B	0016887	molecular_function	ATP hydrolysis activity
B	0020014	biological_process	schizogony
B	0070360	biological_process	symbiont-mediated actin polymerization-dependent cell-to-cell migration in host
B	0085017	biological_process	entry into host cell by a symbiont-containing vacuole
C	0005200	molecular_function	structural constituent of cytoskeleton
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005634	cellular_component	nucleus
C	0005737	cellular_component	cytoplasm
C	0005856	cellular_component	cytoskeleton
C	0005884	cellular_component	actin filament
C	0007010	biological_process	cytoskeleton organization
C	0009665	biological_process	plastid inheritance
C	0015629	cellular_component	actin cytoskeleton
C	0016787	molecular_function	hydrolase activity
C	0016887	molecular_function	ATP hydrolysis activity
C	0020014	biological_process	schizogony
C	0070360	biological_process	symbiont-mediated actin polymerization-dependent cell-to-cell migration in host
C	0085017	biological_process	entry into host cell by a symbiont-containing vacuole
D	0005200	molecular_function	structural constituent of cytoskeleton
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0005634	cellular_component	nucleus
D	0005737	cellular_component	cytoplasm
D	0005856	cellular_component	cytoskeleton
D	0005884	cellular_component	actin filament
D	0007010	biological_process	cytoskeleton organization
D	0009665	biological_process	plastid inheritance
D	0015629	cellular_component	actin cytoskeleton
D	0016787	molecular_function	hydrolase activity
D	0016887	molecular_function	ATP hydrolysis activity
D	0020014	biological_process	schizogony
D	0070360	biological_process	symbiont-mediated actin polymerization-dependent cell-to-cell migration in host
D	0085017	biological_process	entry into host cell by a symbiont-containing vacuole
E	0005200	molecular_function	structural constituent of cytoskeleton
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0005634	cellular_component	nucleus
E	0005737	cellular_component	cytoplasm
E	0005856	cellular_component	cytoskeleton
E	0005884	cellular_component	actin filament
E	0007010	biological_process	cytoskeleton organization
E	0009665	biological_process	plastid inheritance
E	0015629	cellular_component	actin cytoskeleton
E	0016787	molecular_function	hydrolase activity
E	0016887	molecular_function	ATP hydrolysis activity
E	0020014	biological_process	schizogony
E	0070360	biological_process	symbiont-mediated actin polymerization-dependent cell-to-cell migration in host
E	0085017	biological_process	entry into host cell by a symbiont-containing vacuole
F	0000146	molecular_function	microfilament motor activity
F	0003774	molecular_function	cytoskeletal motor activity
F	0003779	molecular_function	actin binding
F	0005515	molecular_function	protein binding
F	0005524	molecular_function	ATP binding
F	0005737	cellular_component	cytoplasm
F	0005886	cellular_component	plasma membrane
F	0007015	biological_process	actin filament organization
F	0015629	cellular_component	actin cytoskeleton
F	0016020	cellular_component	membrane
F	0016459	cellular_component	myosin complex
F	0020039	cellular_component	pellicle
F	0051015	molecular_function	actin filament binding
F	0070258	cellular_component	inner membrane pellicle complex
F	0160055	cellular_component	glideosome

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	PHE54-GLY64

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

Chain	Residue	Details
A	TRP357-GLU365

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

Chain	Residue	Details
A	LEU105-ARG117

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
F	GLY191
B	GLY303
C	SER15
C	GLY16
C	ASP158
C	LYS214
C	GLY303
D	SER15
D	GLY16
D	ASP158
D	LYS214
A	GLY16
D	GLY303
E	SER15
E	GLY16
E	ASP158
E	LYS214
E	GLY303
A	ASP158
A	LYS214
A	GLY303
B	SER15
B	GLY16
B	ASP158
B	LYS214

site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: Phosphoserine; by PKG => ECO:0000269\|PubMed:26149123

Chain	Residue	Details
F	SEP19
B	ASN17
C	ASN17
D	ASN17
E	ASN17

site_id	SWS_FT_FI3
Number of Residues	5
Details	BINDING: BINDING => ECO:0000269\|PubMed:24743229, ECO:0000269\|PubMed:28695858, ECO:0000269\|PubMed:28923924, ECO:0000269\|PubMed:31199804, ECO:0000269\|PubMed:33767187, ECO:0000269\|Ref.7, ECO:0007744\|PDB:4CBU, ECO:0007744\|PDB:5MVV, ECO:0007744\|PDB:5OGW, ECO:0007744\|PDB:6I4D, ECO:0007744\|PDB:6I4E, ECO:0007744\|PDB:6TU4, ECO:0007744\|PDB:7ALN

Chain	Residue	Details
A	LYS19
B	LYS19
C	LYS19
D	LYS19
E	LYS19

site_id	SWS_FT_FI4
Number of Residues	5
Details	BINDING: BINDING => ECO:0000269\|PubMed:24743229, ECO:0000269\|PubMed:28695858, ECO:0000269\|PubMed:31199804, ECO:0007744\|PDB:4CBU, ECO:0007744\|PDB:5MVV, ECO:0007744\|PDB:6I4D

Chain	Residue	Details
A	GLY159
B	GLY159
C	GLY159
D	GLY159
E	GLY159

site_id	SWS_FT_FI5
Number of Residues	5
Details	BINDING: BINDING => ECO:0000269\|PubMed:24743229, ECO:0000269\|PubMed:28695858, ECO:0000269\|PubMed:28923924, ECO:0000269\|PubMed:31199804, ECO:0007744\|PDB:4CBU, ECO:0007744\|PDB:5MVV, ECO:0007744\|PDB:5OGW, ECO:0007744\|PDB:6I4D

Chain	Residue	Details
A	VAL160
B	VAL160
C	VAL160
D	VAL160
E	VAL160

site_id	SWS_FT_FI6
Number of Residues	5
Details	BINDING: BINDING => ECO:0000269\|PubMed:24743229, ECO:0000269\|PubMed:28695858, ECO:0000269\|PubMed:31199804, ECO:0007744\|PDB:4CBU, ECO:0007744\|PDB:5MVV, ECO:0007744\|PDB:6I4D, ECO:0007744\|PDB:6I4E

Chain	Residue	Details
A	GLU215
B	GLU215
C	GLU215
D	GLU215
E	GLU215

site_id	SWS_FT_FI7
Number of Residues	5
Details	SITE: Not methylated => ECO:0000269\|PubMed:31199804

Chain	Residue	Details
A	HIS74
B	HIS74
C	HIS74
D	HIS74
E	HIS74

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