Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6I4F

Crystal Structure of Plasmodium falciparum actin I (A272W mutant) in the Mg-K-ATP/ADP state

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
G	0051015	molecular_function	actin filament binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	30
Details	binding site for residue ATP A 401

Chain	Residue
A	GLY14
A	GLY183
A	ARG211
A	LYS214
A	GLU215
A	GLY303
A	THR304
A	MET306
A	TYR307
A	LYS337
A	ADP402
A	SER15
A	MG403
A	K404
A	HOH505
A	HOH510
A	HOH527
A	HOH537
A	HOH562
A	HOH565
A	HOH602
A	HOH634
A	GLY16
A	HOH707
A	ASN17
A	LYS19
A	GLY157
A	ASP158
A	GLY159
A	VAL160

site_id	AC2
Number of Residues	29
Details	binding site for residue ADP A 402

Chain	Residue
A	GLY14
A	SER15
A	GLY16
A	ASN17
A	LYS19
A	GLY157
A	ASP158
A	GLY183
A	ARG211
A	LYS214
A	GLU215
A	GLY302
A	GLY303
A	THR304
A	MET306
A	TYR307
A	LYS337
A	ATP401
A	MG403
A	HOH510
A	HOH527
A	HOH537
A	HOH562
A	HOH565
A	HOH577
A	HOH602
A	HOH634
A	HOH725
A	HOH784

site_id	AC3
Number of Residues	7
Details	binding site for residue MG A 403

Chain	Residue
A	ATP401
A	ADP402
A	HOH535
A	HOH537
A	HOH565
A	HOH577
A	HOH725

site_id	AC4
Number of Residues	6
Details	binding site for residue K A 404

Chain	Residue
A	ASP155
A	GLY157
A	VAL160
A	ATP401
A	HOH537
A	HOH600

site_id	AC5
Number of Residues	8
Details	binding site for residue BTB A 405

Chain	Residue
A	ARG29
A	SER30
A	ASN93
A	GLU94
A	ARG96
A	HOH543
A	HOH698
A	HOH788

site_id	AC6
Number of Residues	9
Details	binding site for residue PEG A 406

Chain	Residue
A	SER145
A	SER146
A	ARG148
A	LYS329
A	VAL331
A	PRO333
A	GLU335
A	HOH666
G	ARG96

site_id	AC7
Number of Residues	4
Details	binding site for residue NA A 407

Chain	Residue
A	LYS292
A	GLY296
A	LYS327
A	HOH838

site_id	AC8
Number of Residues	7
Details	binding site for residue CL A 408

Chain	Residue
A	HOH818
A	THR319
A	THR320
A	ALA322
A	SER324
A	HOH576
A	HOH815

site_id	AC9
Number of Residues	6
Details	binding site for residue CA G 201

Chain	Residue
G	GLY41
G	ASP42
G	GLU73
G	VAL121
G	HOH388
G	HOH395

site_id	AD1
Number of Residues	6
Details	binding site for residue CA G 202

Chain	Residue
A	GLU168
G	ASP85
G	GLY90
G	ALA92
G	HOH354
G	HOH377

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	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":"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_FI2
Number of Residues	1
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_FI3
Number of Residues	1
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_FI4
Number of Residues	1
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_FI5
Number of Residues	1
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_FI6
Number of Residues	1
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_FI7
Number of Residues	1
Details	Site: {"description":"Not methylated","evidences":[{"source":"PubMed","id":"31199804","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	81
Details	Repeat: {"description":"Gelsolin-like 1","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	123
Details	Region: {"description":"Actin-severing","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	3
Details	Region: {"description":"Actin-actin interfilament contact point"}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	4
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":"4CBW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4CBX","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":"6I4F","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6I4G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6I4H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6I4I","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6I4J","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6I4K","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6I4L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6I4M","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"24743229","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31199804","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4CBU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4CBW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4CBX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6I4D","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6I4E","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6I4F","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6I4H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6I4I","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6I4J","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6I4K","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6I4L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6I4M","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	7
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P06396","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)