Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6I4E

Crystal Structure of Plasmodium falciparum actin I in the Mg-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	0070360	biological_process	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	28
Details	binding site for residue ADP A 401

Chain	Residue
A	GLY14
A	LYS214
A	GLU215
A	GLY302
A	GLY303
A	THR304
A	MET306
A	TYR307
A	LYS337
A	MG402
A	HOH523
A	SER15
A	HOH539
A	HOH543
A	HOH560
A	HOH562
A	HOH587
A	HOH599
A	HOH612
A	HOH651
A	HOH665
A	GLY16
A	ASN17
A	LYS19
A	GLY157
A	ASP158
A	GLY183
A	ARG211

site_id	AC2
Number of Residues	6
Details	binding site for residue MG A 402

Chain	Residue
A	ADP401
A	HOH543
A	HOH547
A	HOH562
A	HOH587
A	HOH612

site_id	AC3
Number of Residues	6
Details	binding site for residue CA A 403

Chain	Residue
A	THR319
A	THR320
A	ALA322
A	SER324
A	HOH692
A	HOH762

site_id	AC4
Number of Residues	4
Details	binding site for residue SCN A 404

Chain	Residue
A	SER235
A	ASP236
A	GLU238
A	LYS239

site_id	AC5
Number of Residues	1
Details	binding site for residue SCN A 405

Chain	Residue
A	HOH694

site_id	AC6
Number of Residues	4
Details	binding site for residue BME A 406

Chain	Residue
A	VAL22
A	ARG29
A	LEU95
A	BTB408

site_id	AC7
Number of Residues	13
Details	binding site for residue BME A 407

Chain	Residue
A	SER142
A	SER145
A	SER146
A	VAL299
A	LEU300
A	SER301
A	PRO333
A	GLU335
A	SER339
A	HOH528
A	HOH556
A	HOH638
A	HOH652

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

Chain	Residue
A	ARG29
A	SER30
A	ASN93
A	GLU94
A	ARG96
A	BME406
A	HOH815

site_id	AC9
Number of Residues	4
Details	binding site for residue CA A 409

Chain	Residue
A	GLU168
G	ASP85
G	GLY90
G	ALA92

site_id	AD1
Number of Residues	6
Details	binding site for residue CA G 201

Chain	Residue
G	GLY41
G	ASP42
G	GLU73
G	VAL121
G	HOH387
G	HOH390

site_id	AD2
Number of Residues	3
Details	binding site for residue PEG G 202

Chain	Residue
G	GLY12
G	TYR87
G	ARG91

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	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:24743229, ECO:0000269\|PubMed:28695858, ECO:0000269\|PubMed:31199804, ECO:0007744\|PDB:4CBU, ECO:0007744\|PDB:4CBW, ECO:0007744\|PDB:4CBX, ECO:0007744\|PDB:5MVV, ECO:0007744\|PDB:6I4D, ECO:0007744\|PDB:6I4E, ECO:0007744\|PDB:6I4F, ECO:0007744\|PDB:6I4G, ECO:0007744\|PDB:6I4H, ECO:0007744\|PDB:6I4I, ECO:0007744\|PDB:6I4J, ECO:0007744\|PDB:6I4K, ECO:0007744\|PDB:6I4L, ECO:0007744\|PDB:6I4M

Chain	Residue	Details
G	GLY41
G	ASP42
G	GLU73
G	VAL121
A	GLY303

site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269\|PubMed:24743229, ECO:0000269\|PubMed:31199804, ECO:0007744\|PDB:4CBU, ECO:0007744\|PDB:4CBW, ECO:0007744\|PDB:4CBX, ECO:0007744\|PDB:6I4D, ECO:0007744\|PDB:6I4E, ECO:0007744\|PDB:6I4F, ECO:0007744\|PDB:6I4H, ECO:0007744\|PDB:6I4I, ECO:0007744\|PDB:6I4J, ECO:0007744\|PDB:6I4K, ECO:0007744\|PDB:6I4L, ECO:0007744\|PDB:6I4M

Chain	Residue	Details
G	ASP85
G	GLY90
G	ALA92

site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
G	LYS111

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0000250\|UniProtKB:P06396

Chain	Residue	Details
G	TYR35

site_id	SWS_FT_FI5
Number of Residues	1
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

site_id	SWS_FT_FI6
Number of Residues	1
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

site_id	SWS_FT_FI7
Number of Residues	1
Details	SITE: Not methylated => ECO:0000269\|PubMed:31199804

Chain	Residue	Details
A	HIS74

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