6I4G

Crystal Structure of Plasmodium falciparum actin I (H74Q) in the Mg-K-ATP 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
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
G	0051015	molecular_function	actin filament binding
H	0051015	molecular_function	actin filament binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	29
Details	binding site for residue ATP A 401

Chain	Residue
A	GLY14
A	GLY183
A	ARG211
A	LYS214
A	GLU215
A	GLY302
A	GLY303
A	THR304
A	MET306
A	TYR307
A	LYS337
A	SER15
A	MG402
A	K403
A	HOH510
A	HOH517
A	HOH525
A	HOH528
A	HOH535
A	HOH544
A	HOH550
A	HOH577
A	GLY16
A	ASN17
A	LYS19
A	GLY157
A	ASP158
A	GLY159
A	VAL160

---

site_id	AC2
Number of Residues	5
Details	binding site for residue MG A 402

Chain	Residue
A	ATP401
A	HOH510
A	HOH525
A	HOH550
A	HOH577

---

site_id	AC3
Number of Residues	5
Details	binding site for residue K A 403

Chain	Residue
A	ASP155
A	GLY157
A	VAL160
A	ATP401
A	HOH503

---

site_id	AC4
Number of Residues	25
Details	binding site for residue ATP B 401

Chain	Residue
B	GLY14
B	SER15
B	GLY16
B	ASN17
B	LYS19
B	GLY157
B	ASP158
B	GLY159
B	VAL160
B	GLY183
B	ARG211
B	LYS214
B	GLU215
B	GLY302
B	GLY303
B	THR304
B	MET306
B	TYR307
B	LYS337
B	MG402
B	K403
B	HOH513
B	HOH519
B	HOH527
B	HOH544

---

site_id	AC5
Number of Residues	5
Details	binding site for residue MG B 402

Chain	Residue
B	ATP401
B	HOH513
B	HOH518
B	HOH519
B	HOH545

---

site_id	AC6
Number of Residues	5
Details	binding site for residue K B 403

Chain	Residue
B	ASP155
B	GLY157
B	VAL160
B	ATP401
B	HOH515

---

site_id	AC7
Number of Residues	2
Details	binding site for residue BME B 404

Chain	Residue
B	VAL371
B	ARG373

---

site_id	AC8
Number of Residues	6
Details	binding site for residue CA G 201

Chain	Residue
G	GLY41
G	ASP42
G	GLU73
G	VAL121
G	HOH344
G	HOH348

---

site_id	AC9
Number of Residues	5
Details	binding site for residue CA G 202

Chain	Residue
B	GLU168
G	ASP85
G	GLY90
G	ALA92
G	HOH327

---

site_id	AD1
Number of Residues	4
Details	binding site for residue BME G 203

Chain	Residue
G	HOH336
H	ASN67
H	GLN99
H	TYR116

---

site_id	AD2
Number of Residues	2
Details	binding site for residue SCN G 204

Chain	Residue
G	TYR44
G	LYS117

---

site_id	AD3
Number of Residues	6
Details	binding site for residue CA H 201

Chain	Residue
H	GLY41
H	ASP42
H	GLU73
H	VAL121
H	HOH340
H	HOH342

---

site_id	AD4
Number of Residues	5
Details	binding site for residue CA H 202

Chain	Residue
A	GLU168
A	HOH608
H	ASP85
H	GLY90
H	ALA92

---

site_id	AD5
Number of Residues	4
Details	binding site for residue BME H 203

Chain	Residue
G	ASN67
G	GLN99
G	GLY100
G	TYR116

---

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	10
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	2
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	2
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	2
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	2
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	2
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	2
Details	Site: {"description":"Not methylated","evidences":[{"source":"PubMed","id":"31199804","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	6
Details	Region: {"description":"Actin-actin interfilament contact point"}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	8
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_FI10
Number of Residues	6
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_FI11
Number of Residues	14
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI12
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P06396","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI13
Number of Residues	81
Details	Repeat: {"description":"Gelsolin-like 1","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI14
Number of Residues	123
Details	Region: {"description":"Actin-severing","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---