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9F1R

Cryo-EM structure of SV2B-Hc-A1 complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0001669cellular_componentacrosomal vesicle
A0005515molecular_functionprotein binding
A0005886cellular_componentplasma membrane
A0006836biological_processneurotransmitter transport
A0007268biological_processchemical synaptic transmission
A0008021cellular_componentsynaptic vesicle
A0016020cellular_componentmembrane
A0022857molecular_functiontransmembrane transporter activity
A0030672cellular_componentsynaptic vesicle membrane
A0031410cellular_componentcytoplasmic vesicle
A0055085biological_processtransmembrane transport
A0099509biological_processregulation of presynaptic cytosolic calcium ion concentration
A2000300biological_processregulation of synaptic vesicle exocytosis
B0005576cellular_componentextracellular region
Functional Information from PROSITE/UniProt
site_idPS00216
Number of Residues17
DetailsSUGAR_TRANSPORT_1 Sugar transport proteins signature 1. LGGLADKLGRKrvlsm.S
ChainResidueDetails
ALEU165-SER181

site_idPS00217
Number of Residues26
DetailsSUGAR_TRANSPORT_2 Sugar transport proteins signature 2. IsGIGiGGalpivfaYfsEflsrekR
ChainResidueDetails
AILE207-ARG232

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues240
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues168
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues42
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q8BG39","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsRegion: {"description":"Interaction with host ganglioside GT1b","evidences":[{"source":"PubMed","id":"18704164","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27958736","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14731268","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2VU9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5TPB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5TPC","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues3
DetailsMotif: {"description":"Host ganglioside-binding motif","evidences":[{"source":"UniProtKB","id":"P0DPI0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18704164","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27958736","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2VU9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5TPB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5TPC","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18704164","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27958736","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14731268","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2VU9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5TPB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5TPC","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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