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8JLI

Cryo-EM structure of SV2A dimer in complex levetiracetam

Functional Information from GO Data
ChainGOidnamespacecontents
A0005783cellular_componentendoplasmic reticulum
A0005886cellular_componentplasma membrane
A0005911cellular_componentcell-cell junction
A0006836biological_processneurotransmitter transport
A0007268biological_processchemical synaptic transmission
A0008021cellular_componentsynaptic vesicle
A0016020cellular_componentmembrane
A0016082biological_processsynaptic vesicle priming
A0019901molecular_functionprotein kinase binding
A0022857molecular_functiontransmembrane transporter activity
A0030672cellular_componentsynaptic vesicle membrane
A0031410cellular_componentcytoplasmic vesicle
A0031594cellular_componentneuromuscular junction
A0043005cellular_componentneuron projection
A0048786cellular_componentpresynaptic active zone
A0055085biological_processtransmembrane transport
A0098793cellular_componentpresynapse
A0098978cellular_componentglutamatergic synapse
A0098982cellular_componentGABA-ergic synapse
B0005783cellular_componentendoplasmic reticulum
B0005886cellular_componentplasma membrane
B0005911cellular_componentcell-cell junction
B0006836biological_processneurotransmitter transport
B0007268biological_processchemical synaptic transmission
B0008021cellular_componentsynaptic vesicle
B0016020cellular_componentmembrane
B0016082biological_processsynaptic vesicle priming
B0019901molecular_functionprotein kinase binding
B0022857molecular_functiontransmembrane transporter activity
B0030672cellular_componentsynaptic vesicle membrane
B0031410cellular_componentcytoplasmic vesicle
B0031594cellular_componentneuromuscular junction
B0043005cellular_componentneuron projection
B0048786cellular_componentpresynaptic active zone
B0055085biological_processtransmembrane transport
B0098793cellular_componentpresynapse
B0098978cellular_componentglutamatergic synapse
B0098982cellular_componentGABA-ergic synapse
Functional Information from PROSITE/UniProt
site_idPS00217
Number of Residues26
DetailsSUGAR_TRANSPORT_2 Sugar transport proteins signature 2. LsGVGiGGsipivfsYfsEflaqekR
ChainResidueDetails
ALEU264-ARG289

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues480
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues348
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues88
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q02563","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q9JIS5","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues6
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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