8JLF

Cryo-EM structure of SV2A in complex with BoNT/A2 Hc

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005783	cellular_component	endoplasmic reticulum
A	0005886	cellular_component	plasma membrane
A	0005911	cellular_component	cell-cell junction
A	0006836	biological_process	neurotransmitter transport
A	0006874	biological_process	intracellular calcium ion homeostasis
A	0007268	biological_process	chemical synaptic transmission
A	0008021	cellular_component	synaptic vesicle
A	0014052	biological_process	regulation of gamma-aminobutyric acid secretion
A	0016020	cellular_component	membrane
A	0016082	biological_process	synaptic vesicle priming
A	0019901	molecular_function	protein kinase binding
A	0022857	molecular_function	transmembrane transporter activity
A	0030425	cellular_component	dendrite
A	0030672	cellular_component	synaptic vesicle membrane
A	0031410	cellular_component	cytoplasmic vesicle
A	0031594	cellular_component	neuromuscular junction
A	0042995	cellular_component	cell projection
A	0043005	cellular_component	neuron projection
A	0043025	cellular_component	neuronal cell body
A	0045202	cellular_component	synapse
A	0048786	cellular_component	presynaptic active zone
A	0055085	biological_process	transmembrane transport
A	0098793	cellular_component	presynapse
A	0098978	cellular_component	glutamatergic synapse
A	0098982	cellular_component	GABA-ergic synapse
B	0005576	cellular_component	extracellular region

Functional Information from PROSITE/UniProt

site_id	PS00217
Number of Residues	26
Details	SUGAR_TRANSPORT_2 Sugar transport proteins signature 2. LsGVGiGGsipivfsYfsEflaqekR

Chain	Residue	Details
A	LEU264-ARG289

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	240
Details	TRANSMEM: Helical => ECO:0000255

Chain	Residue	Details
A	PHE170-LEU190
A	ILE652-LEU672
A	PHE686-VAL708
A	ALA713-LEU731
A	MET206-ALA226
A	CYS234-GLY254
A	LEU263-PHE283
A	TRP295-ILE315
A	VAL335-PRO355
A	LEU448-PHE468
A	PHE599-MET619
A	MET627-SER647

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site_id	SWS_FT_FI2
Number of Residues	174
Details	TOPO_DOM: Extracellular => ECO:0000255

Chain	Residue	Details
A	PRO191-GLY205
A	TYR255-ARG262
A	PRO316-ARG334
A	PRO469-TYR598
A	GLU648-MET651
A	GLY709-LYS712

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site_id	SWS_FT_FI3
Number of Residues	135
Details	TOPO_DOM: Cytoplasmic => ECO:0000255

Chain	Residue	Details
A	ASP227-GLN233
A	LEU284-SER294
A	GLU356-THR447
A	ASP620-ARG626
A	THR673-ALA685
A	LYS732-GLN742

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site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332

Chain	Residue	Details
A	SER80
A	SER81

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:19690332

Chain	Residue	Details
A	THR84

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site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9JIS5

Chain	Residue	Details
A	SER127

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site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q02563

Chain	Residue	Details
A	SER393

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site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q9JIS5

Chain	Residue	Details
A	TYR480

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site_id	SWS_FT_FI9
Number of Residues	3
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASN498
A	ASN548
A	ASN573

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