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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6I4K

Crystal Structure of Plasmodium falciparum actin I (G115A mutant) in the Ca-ATP 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	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	27
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	CA402
A	HOH550
A	HOH557
A	HOH575
A	HOH583
A	HOH626
A	HOH636
A	HOH641
A	GLY16
A	ASN17
A	LYS19
A	GLY157
A	ASP158
A	GLY159
A	VAL160

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

Chain	Residue
A	ATP401
A	HOH557
A	HOH569
A	HOH600
A	HOH602
A	HOH641

site_id	AC3
Number of Residues	4
Details	binding site for residue SCN A 403

Chain	Residue
A	VAL22
A	PRO173
A	BTB404
A	HOH765

site_id	AC4
Number of Residues	9
Details	binding site for residue BTB A 404

Chain	Residue
A	SER30
A	ASN93
A	GLU94
A	ARG96
A	SCN403
A	HOH513
A	HOH654
A	HOH757
A	HOH765

site_id	AC5
Number of Residues	7
Details	binding site for residue PEG A 405

Chain	Residue
A	ALA53
A	PHE54
A	VAL55
A	GLU58
A	LYS85
A	HIS89
A	ASN93

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

Chain	Residue
A	THR319
A	THR320
A	ALA322
A	SER324

site_id	AC7
Number of Residues	6
Details	binding site for residue CA G 201

Chain	Residue
G	GLY41
G	ASP42
G	GLU73
G	VAL121
G	HOH363
G	HOH386

site_id	AC8
Number of Residues	6
Details	binding site for residue CA G 202

Chain	Residue
A	GLU168
G	ASP85
G	GLY90
G	ALA92
G	HOH374
G	HOH378

site_id	AC9
Number of Residues	6
Details	binding site for residue SCN G 203

Chain	Residue
G	PRO31
G	PHE39
G	TYR44
G	HOH303
G	HOH338
G	HOH440

site_id	AD1
Number of Residues	4
Details	binding site for residue BME G 204

Chain	Residue
G	GLY12
G	LYS13
G	TYR59
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. LLTEApLNPkaNR

Chain	Residue	Details
A	LEU105-ARG117

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	5
Details	BINDING: BINDING => ECO:0000269\|PubMed:24743229, ECO:0000269\|PubMed:28695858, ECO:0000269\|PubMed:31199804, ECO:0000269\|PubMed:33767187, ECO:0000269\|Ref.7, ECO:0007744\|PDB:4CBU, ECO:0007744\|PDB:5MVV, ECO:0007744\|PDB:6I4D, ECO:0007744\|PDB:6I4E, ECO:0007744\|PDB:6TU4, ECO:0007744\|PDB:7ALN

Chain	Residue	Details
A	SER15
A	GLY16
A	ASP158
A	LYS214
A	GLY303

site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269\|PubMed:24743229, ECO:0000269\|PubMed:28695858, ECO:0000269\|PubMed:28923924, ECO:0000269\|PubMed:31199804, 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

Chain	Residue	Details
A	ASN17

site_id	SWS_FT_FI3
Number of Residues	1
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

site_id	SWS_FT_FI4
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

Chain	Residue	Details
A	GLY159

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

219140

PDB entries from 2024-05-01

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