Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

9F3C

Low-resolution (5.4 angstrom) cryo-EM structure of SV2B-BoNT/A1 at pH 5.5

Functional Information from GO Data
ChainGOidnamespacecontents
A0001669cellular_componentacrosomal vesicle
A0005515molecular_functionprotein binding
A0005886cellular_componentplasma membrane
A0006836biological_processneurotransmitter transport
A0008021cellular_componentsynaptic vesicle
A0016020cellular_componentmembrane
A0030672cellular_componentsynaptic vesicle membrane
A0031410cellular_componentcytoplasmic vesicle
A0045202cellular_componentsynapse
A0099509biological_processregulation of presynaptic cytosolic calcium ion concentration
A2000300biological_processregulation of synaptic vesicle exocytosis
B0004222molecular_functionmetalloendopeptidase activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0008237molecular_functionmetallopeptidase activity
B0008270molecular_functionzinc ion binding
B0008289molecular_functionlipid binding
B0008320molecular_functionprotein transmembrane transporter activity
B0016020cellular_componentmembrane
B0016787molecular_functionhydrolase activity
B0020002cellular_componenthost cell plasma membrane
B0030430cellular_componenthost cell cytoplasm
B0033644cellular_componenthost cell membrane
B0044161cellular_componenthost cell cytoplasmic vesicle
B0044164cellular_componenthost cell cytosol
B0044221cellular_componenthost cell synapse
B0044231cellular_componenthost cell presynaptic membrane
B0046872molecular_functionmetal ion binding
B0071806biological_processprotein transmembrane transport
B0090729molecular_functiontoxin activity
B0141157biological_processsymbiont-mediated suppression of host exocytosis
B1905576molecular_functionganglioside GT1b binding
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 Residues40
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
BILE627-LEU647
BLEU656-LEU676
ALEU227-SER237
AGLU299-THR390
AALA557-ARG565
ATHR614-ALA626
AARG673-MET683

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10095
ChainResidueDetails
BGLN224
AILE593-ILE613
APHE627-VAL649
AVAL654-LEU672
AMET149-ALA169
AALA183-PHE203
ALEU206-PHE226
ATRP238-ILE258
AVAL278-PRO298
ALEU391-PHE411
APHE536-SER556
ALEU566-GLY586

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:17173035, ECO:0000305|PubMed:9783750, ECO:0007744|PDB:2NYY, ECO:0007744|PDB:2NZ9, ECO:0007744|PDB:3BTA, ECO:0007744|PDB:3QIX, ECO:0007744|PDB:3QIY, ECO:0007744|PDB:3QIZ, ECO:0007744|PDB:3QJ0
ChainResidueDetails
BHIS223
BHIS227
APRO259-ARG277
APRO412-ASP535
AASN587-MET592
AGLY650-LYS653

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:17173035, ECO:0007744|PDB:2NYY, ECO:0007744|PDB:2NZ9, ECO:0007744|PDB:3BTA, ECO:0007744|PDB:3QIX, ECO:0007744|PDB:3QIY, ECO:0007744|PDB:3QIZ, ECO:0007744|PDB:3QJ0
ChainResidueDetails
BGLU262

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:18704164, ECO:0000269|PubMed:27958736, ECO:0007744|PDB:2VU9, ECO:0007744|PDB:5TPB, ECO:0007744|PDB:5TPC
ChainResidueDetails
BTYR1117

site_idSWS_FT_FI6
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:18704164, ECO:0000269|PubMed:27958736, ECO:0000305|PubMed:14731268, ECO:0007744|PDB:2VU9, ECO:0007744|PDB:5TPB, ECO:0007744|PDB:5TPC
ChainResidueDetails
BGLU1203

site_idSWS_FT_FI7
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000305|PubMed:11827515
ChainResidueDetails
BALA363
BPHE366
AASN516

237735

PDB entries from 2025-06-18

PDB statisticsPDBj update infoContact PDBjnumon