Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6TU4

Structure of Plasmodium Actin1 filament

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
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	0051701	biological_process	biological process involved in interaction with host
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	0000166	molecular_function	nucleotide binding
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	0051701	biological_process	biological process involved in interaction with host
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	0000166	molecular_function	nucleotide binding
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	0051701	biological_process	biological process involved in interaction with host
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	0000166	molecular_function	nucleotide binding
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	0051701	biological_process	biological process involved in interaction with host
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
F	0000166	molecular_function	nucleotide binding
F	0005200	molecular_function	structural constituent of cytoskeleton
F	0005515	molecular_function	protein binding
F	0005524	molecular_function	ATP binding
F	0005634	cellular_component	nucleus
F	0005737	cellular_component	cytoplasm
F	0005856	cellular_component	cytoskeleton
F	0005884	cellular_component	actin filament
F	0007010	biological_process	cytoskeleton organization
F	0009665	biological_process	plastid inheritance
F	0015629	cellular_component	actin cytoskeleton
F	0016787	molecular_function	hydrolase activity
F	0016887	molecular_function	ATP hydrolysis activity
F	0020014	biological_process	schizogony
F	0051701	biological_process	biological process involved in interaction with host
F	0070360	biological_process	symbiont-mediated actin polymerization-dependent cell-to-cell migration in host
F	0085017	biological_process	entry into host cell by a symbiont-containing vacuole

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue MG A 401

Chain	Residue
A	ADP403
A	HOH512
A	HOH513
A	HOH514
A	HOH520
A	HOH525

site_id	AC2
Number of Residues	8
Details	binding site for residue 9UE A 402

Chain	Residue
A	TYR199
A	GLY200
A	GLU206
A	ILE248
D	ASP180
A	HIS195
A	ARG197
A	GLY198

site_id	AC3
Number of Residues	15
Details	binding site for residue ADP A 403

Chain	Residue
A	GLY14
A	SER15
A	GLY16
A	ASN17
A	LYS19
A	ASP158
A	LYS214
A	GLU215
A	GLY303
A	TYR307
A	MG401
A	HOH513
A	HOH514
A	HOH520
A	HOH525

site_id	AC4
Number of Residues	6
Details	binding site for residue MG B 401

Chain	Residue
B	ADP403
B	HOH504
B	HOH508
B	HOH512
B	HOH514
B	HOH517

site_id	AC5
Number of Residues	9
Details	binding site for residue 9UE B 402

Chain	Residue
A	HIS74
A	ASP180
B	HIS195
B	ARG197
B	GLY198
B	TYR199
B	GLY200
B	GLU206
B	LEU243

site_id	AC6
Number of Residues	17
Details	binding site for residue ADP B 403

Chain	Residue
B	GLY14
B	SER15
B	GLY16
B	ASN17
B	LYS19
B	GLY157
B	ASP158
B	LYS214
B	GLU215
B	GLY303
B	TYR307
B	MG401
B	HOH504
B	HOH512
B	HOH514
B	HOH516
B	HOH517

site_id	AC7
Number of Residues	6
Details	binding site for residue MG C 401

Chain	Residue
C	ADP403
C	HOH504
C	HOH510
C	HOH514
C	HOH515
C	HOH518

site_id	AC8
Number of Residues	9
Details	binding site for residue 9UE C 402

Chain	Residue
B	ILE76
B	ASP180
C	ARG197
C	GLY198
C	TYR199
C	GLY200
C	GLU206
C	LEU243
C	ILE248

site_id	AC9
Number of Residues	16
Details	binding site for residue ADP C 403

Chain	Residue
C	GLY14
C	SER15
C	GLY16
C	ASN17
C	LYS19
C	GLY157
C	ASP158
C	LYS214
C	GLU215
C	GLY303
C	TYR307
C	MG401
C	HOH510
C	HOH514
C	HOH515
C	HOH518

site_id	AD1
Number of Residues	6
Details	binding site for residue MG D 401

Chain	Residue
D	ADP403
D	HOH507
D	HOH511
D	HOH515
D	HOH521
D	HOH522

site_id	AD2
Number of Residues	6
Details	binding site for residue 9UE D 402

Chain	Residue
D	ARG197
D	GLY198
D	TYR199
D	GLY200
F	ASP180
D	HIS195

site_id	AD3
Number of Residues	16
Details	binding site for residue ADP D 403

Chain	Residue
D	GLY14
D	SER15
D	GLY16
D	ASN17
D	LYS19
D	GLY157
D	ASP158
D	LYS214
D	GLU215
D	GLY303
D	TYR307
D	MG401
D	HOH507
D	HOH515
D	HOH521
D	HOH522

site_id	AD4
Number of Residues	6
Details	binding site for residue MG F 401

Chain	Residue
F	ADP403
F	HOH510
F	HOH511
F	HOH512
F	HOH517
F	HOH519

site_id	AD5
Number of Residues	7
Details	binding site for residue 9UE F 402

Chain	Residue
F	HIS195
F	ARG197
F	GLY198
F	TYR199
F	GLY200
F	GLU206
F	LEU243

site_id	AD6
Number of Residues	15
Details	binding site for residue ADP F 403

Chain	Residue
F	GLY14
F	SER15
F	GLY16
F	ASN17
F	LYS19
F	GLY157
F	ASP158
F	LYS214
F	GLU215
F	GLY303
F	MG401
F	HOH510
F	HOH512
F	HOH517
F	HOH519

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	105
Details	Region: {"description":"DNAseI-binding D loop; regulates polymerization and stability of the actin filament","evidences":[{"source":"UniProtKB","id":"Q4Z1L3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	25
Details	Binding site: {"evidences":[{"source":"PubMed","id":"24743229","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28695858","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31199804","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"33767187","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2020","submissionDatabase":"PDB data bank","title":"Malaria parasite actomyosin rigor-state structure at near-atomic resolution.","authors":["Vahokoski J.","Calder L.J.","Lopez A.J.","Molloy J.E.","Rosenthal P.B.","Kursula I."]}},{"source":"PDB","id":"4CBU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5MVV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6I4D","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6I4E","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6TU4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7ALN","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	5
Details	Binding site: {"evidences":[{"source":"PubMed","id":"24743229","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28695858","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28923924","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31199804","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2020","submissionDatabase":"PDB data bank","title":"Malaria parasite actomyosin rigor-state structure at near-atomic resolution.","authors":["Vahokoski J.","Calder L.J.","Lopez A.J.","Molloy J.E.","Rosenthal P.B.","Kursula I."]}},{"source":"PDB","id":"4CBU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5MVV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5OGW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6I4D","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6I4E","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6TU4","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	5
Details	Binding site: {"evidences":[{"source":"PubMed","id":"24743229","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28695858","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28923924","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31199804","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"33767187","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2020","submissionDatabase":"PDB data bank","title":"Malaria parasite actomyosin rigor-state structure at near-atomic resolution.","authors":["Vahokoski J.","Calder L.J.","Lopez A.J.","Molloy J.E.","Rosenthal P.B.","Kursula I."]}},{"source":"PDB","id":"4CBU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5MVV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5OGW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6I4D","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6I4E","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6TU4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7ALN","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	5
Details	Binding site: {"evidences":[{"source":"PubMed","id":"24743229","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28695858","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31199804","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4CBU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5MVV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6I4D","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	5
Details	Binding site: {"evidences":[{"source":"PubMed","id":"24743229","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28695858","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28923924","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31199804","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4CBU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5MVV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5OGW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6I4D","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	5
Details	Binding site: {"evidences":[{"source":"PubMed","id":"24743229","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28695858","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31199804","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4CBU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5MVV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6I4D","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6I4E","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	5
Details	Site: {"description":"Not methylated","evidences":[{"source":"PubMed","id":"31199804","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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