4M63

Crystal Structure of a Filament-Like Actin Trimer Bound to the Bacterial Effector VopL

Functional Information from GO Data

Chain	GOid	namespace	contents
C	0000281	biological_process	mitotic cytokinesis
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0005856	cellular_component	cytoskeleton
C	0006338	biological_process	chromatin remodeling
C	0007291	biological_process	sperm individualization
C	0016787	molecular_function	hydrolase activity
C	0030723	biological_process	ovarian fusome organization
C	0031011	cellular_component	Ino80 complex
C	0032507	biological_process	maintenance of protein location in cell
C	0035060	cellular_component	brahma complex
C	0035148	biological_process	tube formation
D	0000281	biological_process	mitotic cytokinesis
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0005856	cellular_component	cytoskeleton
D	0006338	biological_process	chromatin remodeling
D	0007291	biological_process	sperm individualization
D	0016787	molecular_function	hydrolase activity
D	0030723	biological_process	ovarian fusome organization
D	0031011	cellular_component	Ino80 complex
D	0032507	biological_process	maintenance of protein location in cell
D	0035060	cellular_component	brahma complex
D	0035148	biological_process	tube formation
E	0000281	biological_process	mitotic cytokinesis
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0005737	cellular_component	cytoplasm
E	0005856	cellular_component	cytoskeleton
E	0006338	biological_process	chromatin remodeling
E	0007291	biological_process	sperm individualization
E	0016787	molecular_function	hydrolase activity
E	0030723	biological_process	ovarian fusome organization
E	0031011	cellular_component	Ino80 complex
E	0032507	biological_process	maintenance of protein location in cell
E	0035060	cellular_component	brahma complex
E	0035148	biological_process	tube formation

Functional Information from PDB Data

site_id	AC1
Number of Residues	18
Details	BINDING SITE FOR RESIDUE ATP C 401

Chain	Residue
C	GLY13
C	GLY182
C	LYS213
C	GLU214
C	GLY302
C	THR303
C	MET305
C	TYR306
C	LYS336
C	CA402
C	SER14
C	GLY15
C	MET16
C	LYS18
C	GLY156
C	ASP157
C	GLY158
C	VAL159

---

site_id	AC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CA C 402

Chain	Residue
C	ATP401

---

site_id	AC3
Number of Residues	19
Details	BINDING SITE FOR RESIDUE ATP D 401

Chain	Residue
D	GLY13
D	SER14
D	GLY15
D	MET16
D	LYS18
D	GLY156
D	ASP157
D	GLY158
D	VAL159
D	ARG210
D	LYS213
D	GLU214
D	GLY301
D	GLY302
D	THR303
D	MET305
D	TYR306
D	LYS336
D	CA402

---

site_id	AC4
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CA D 402

Chain	Residue
D	ATP401

---

site_id	AC5
Number of Residues	18
Details	BINDING SITE FOR RESIDUE ATP E 401

Chain	Residue
E	GLY13
E	SER14
E	GLY15
E	MET16
E	LYS18
E	GLN137
E	GLY156
E	ASP157
E	VAL159
E	GLY182
E	LYS213
E	GLU214
E	GLY301
E	GLY302
E	THR303
E	MET305
E	LYS336
E	CA402

---

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CA E 402

Chain	Residue
E	ASP11
E	GLN137
E	ATP401

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
C	TYR53-GLY63

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site_id	PS00432
Number of Residues	9
Details	ACTINS_2 Actins signature 2. WISKqEYDE

Chain	Residue	Details
C	TRP356-GLU364

---

site_id	PS01132
Number of Residues	13
Details	ACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR

Chain	Residue	Details
C	LEU104-ARG116

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	MOD_RES: N-acetylaspartate => ECO:0000250

Chain	Residue	Details
C	ASP2
D	ASP2
E	ASP2

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	MOD_RES: Methionine sulfoxide => ECO:0000269|PubMed:22116028

Chain	Residue	Details
C	MET44
C	MET47
D	MET44
D	MET47
E	MET44
E	MET47

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	MOD_RES: Tele-methylhistidine => ECO:0000250|UniProtKB:P02572

Chain	Residue	Details
C	HIS73
D	HIS73
E	HIS73

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