4CBX

Crystal structure of Plasmodium berghei actin II

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005856	cellular_component	cytoskeleton
A	0016787	molecular_function	hydrolase activity
A	0016887	molecular_function	ATP hydrolysis activity
A	0035891	biological_process	exit from host cell
A	0044129	biological_process	positive regulation of development of symbiont in host
A	0044782	biological_process	cilium organization
A	0048232	biological_process	male gamete generation
G	0051015	molecular_function	actin filament binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 1378

Chain	Residue
A	ATP1374
A	HOH2003
A	HOH2005
A	HOH2006
A	HOH2085
A	HOH2099

---

site_id	AC2
Number of Residues	25
Details	BINDING SITE FOR RESIDUE ATP A 1374

Chain	Residue
A	MET16
A	LYS18
A	GLY156
A	ASP157
A	GLY158
A	VAL159
A	GLY182
A	ARG210
A	LYS213
A	GLU214
A	GLY302
A	GLY303
A	THR304
A	MET306
A	LYS337
A	CA1378
A	HOH2006
A	HOH2099
A	HOH2101
A	HOH2105
A	HOH2143
A	HOH2229
A	GLY13
A	SER14
A	GLY15

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 1375

Chain	Residue
A	ARG270
A	GLU271
A	CYS272
A	HOH2178

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 G 1150

Chain	Residue
A	ARG147
A	LYS329
A	HOH2094
G	ARG120
G	HOH2096

---

site_id	AC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 A 1376

Chain	Residue
A	TYR309
A	ILE310
A	GLY311
A	GLU312
A	HOH2201
A	HOH2202
A	HOH2206
A	HOH2224
A	HOH2245

---

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE NA A 1377

Chain	Residue
A	ASN296
A	ASN297
A	HOH2248

---

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA G 1151

Chain	Residue
A	GLU167
A	HOH2111
G	ASP109
G	GLY114
G	ALA116

---

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA G 1152

Chain	Residue
G	GLY65
G	ASP66
G	GLU97
G	VAL145
G	HOH2045
G	HOH2046

---

Functional Information from PROSITE/UniProt

site_id	PS00406
Number of Residues	11
Details	ACTINS_1 Actins signature 1. YVGDEAQn.KRG

Chain	Residue	Details
A	TYR53-GLY63

---

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. LLTEApLNPktNR

Chain	Residue	Details
A	LEU104-ARG116

---

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	ASP66
G	GLU97
G	VAL145
A	ASP157
A	LYS213
A	GLY303
G	GLY65

---

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	GLY114
G	ALA116
G	ASP109

---

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

Chain	Residue	Details
G	LYS135

---

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

Chain	Residue	Details
G	TYR59

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