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7UDB

Cryo-EM structure of a synaptobrevin-Munc18-1-syntaxin-1 complex class 2

Functional Information from GO Data
ChainGOidnamespacecontents
A0000149molecular_functionSNARE binding
A0002576biological_processplatelet degranulation
A0003006biological_processdevelopmental process involved in reproduction
A0005515molecular_functionprotein binding
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006886biological_processintracellular protein transport
A0006887biological_processexocytosis
A0006904biological_processvesicle docking involved in exocytosis
A0007269biological_processneurotransmitter secretion
A0007274biological_processneuromuscular synaptic transmission
A0007412biological_processaxon target recognition
A0010807biological_processregulation of synaptic vesicle priming
A0015031biological_processprotein transport
A0016020cellular_componentmembrane
A0016082biological_processsynaptic vesicle priming
A0016188biological_processsynaptic vesicle maturation
A0016192biological_processvesicle-mediated transport
A0017075molecular_functionsyntaxin-1 binding
A0019901molecular_functionprotein kinase binding
A0019904molecular_functionprotein domain specific binding
A0019905molecular_functionsyntaxin binding
A0030141cellular_componentsecretory granule
A0030424cellular_componentaxon
A0031091cellular_componentplatelet alpha granule
A0031333biological_processnegative regulation of protein-containing complex assembly
A0031338biological_processregulation of vesicle fusion
A0032229biological_processnegative regulation of synaptic transmission, GABAergic
A0032355biological_processresponse to estradiol
A0032991cellular_componentprotein-containing complex
A0035493biological_processSNARE complex assembly
A0035544biological_processnegative regulation of SNARE complex assembly
A0042802molecular_functionidentical protein binding
A0043195cellular_componentterminal bouton
A0043274molecular_functionphospholipase binding
A0043306biological_processpositive regulation of mast cell degranulation
A0043524biological_processnegative regulation of neuron apoptotic process
A0045335cellular_componentphagocytic vesicle
A0045921biological_processpositive regulation of exocytosis
A0045956biological_processpositive regulation of calcium ion-dependent exocytosis
A0048471cellular_componentperinuclear region of cytoplasm
A0048787cellular_componentpresynaptic active zone membrane
A0050821biological_processprotein stabilization
A0051402biological_processneuron apoptotic process
A0051649biological_processestablishment of localization in cell
A0060090molecular_functionmolecular adaptor activity
A0060292biological_processlong-term synaptic depression
A0070527biological_processplatelet aggregation
A0071346biological_processcellular response to type II interferon
A0072659biological_processprotein localization to plasma membrane
A0098688cellular_componentparallel fiber to Purkinje cell synapse
A0098793cellular_componentpresynapse
A0098794cellular_componentpostsynapse
A0098831cellular_componentpresynaptic active zone cytoplasmic component
A0098888cellular_componentextrinsic component of presynaptic membrane
A0098978cellular_componentglutamatergic synapse
A0099523cellular_componentpresynaptic cytosol
A0099525biological_processpresynaptic dense core vesicle exocytosis
A0106022biological_processpositive regulation of vesicle docking
A1903296biological_processpositive regulation of glutamate secretion, neurotransmission
A2000367biological_processregulation of acrosomal vesicle exocytosis
B0016020cellular_componentmembrane
B0016192biological_processvesicle-mediated transport
C0016020cellular_componentmembrane
C0016192biological_processvesicle-mediated transport
Functional Information from PROSITE/UniProt
site_idPS00417
Number of Residues20
DetailsSYNAPTOBREVIN Synaptobrevin signature. NVDKVlERdqKLSeLdDRAD
ChainResidueDetails
CASN49-ASP68

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsSITE: (Microbial infection) Cleavage; by C.botulinum neurotoxin type F (BoNT/F, botF) => ECO:0000269|PubMed:8505288
ChainResidueDetails
CGLN58
ASER509
ASER593

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: (Microbial infection) Cleavage; by C.botulinum neurotoxin type D (BoNT/D, botD) => ECO:0000269|PubMed:8175689
ChainResidueDetails
CLYS59
BSER64
BSER95

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: (Microbial infection) Cleavage; by C.botulinum neurotoxin type X (BoNT/X) => ECO:0000269|PubMed:28770820
ChainResidueDetails
CARG66

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: (Microbial infection) Cleavage; by C.tetani tetanus toxin (tetX) => ECO:0000269|PubMed:1331807
ChainResidueDetails
CGLN76
BLYS253

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: (Microbial infection) Cleavage; by C.botulinum neurotoxin type G (BoNT/G, botG) => ECO:0000269|PubMed:7910017
ChainResidueDetails
CALA81

227344

PDB entries from 2024-11-13

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