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6G5F

Crystal structure of an engineered Botulinum Neurotoxin type B mutant E1191M/S1199Y in complex with human synaptotagmin 1

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0008289molecular_functionlipid binding
A0008320molecular_functionprotein transmembrane transporter activity
A0016787molecular_functionhydrolase activity
A0035821biological_processmodulation of process of another organism
A0044161cellular_componenthost cell cytoplasmic vesicle
A0044164cellular_componenthost cell cytosol
A0044231cellular_componenthost cell presynaptic membrane
A0046872molecular_functionmetal ion binding
A0071806biological_processprotein transmembrane transport
A0090729molecular_functiontoxin activity
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
B0016787molecular_functionhydrolase activity
B0035821biological_processmodulation of process of another organism
B0044161cellular_componenthost cell cytoplasmic vesicle
B0044164cellular_componenthost cell cytosol
B0044231cellular_componenthost cell presynaptic membrane
B0046872molecular_functionmetal ion binding
B0071806biological_processprotein transmembrane transport
B0090729molecular_functiontoxin activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue GOL A 1301
ChainResidue
AASP69
AGLN259
ASER375
BGLU452
BMLI1301

site_idAC2
Number of Residues4
Detailsbinding site for residue GOL A 1302
ChainResidue
AGLN207
AGLN275
BLEU705
BASN709

site_idAC3
Number of Residues3
Detailsbinding site for residue GOL A 1303
ChainResidue
AARG123
AVAL124
AASN130

site_idAC4
Number of Residues10
Detailsbinding site for residue MLI B 1301
ChainResidue
AGLN259
APHE374
AASP376
AGOL1301
BGLU452
BLEU454
BPHE456
BTHR710
BTYR713
BTHR714

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10932256","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1429690","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1EPW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1F31","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2NP0","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10932256","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1EPW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1F31","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2NP0","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues415
DetailsRegion: {"description":"Translocation domain (TD)","evidences":[{"source":"UniProtKB","id":"P0DPI0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues51
DetailsRegion: {"description":"Belt; not required for channel formation","evidences":[{"source":"PubMed","id":"10932256","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues3
DetailsMotif: {"description":"Host ganglioside-binding motif","evidences":[{"source":"PubMed","id":"10932256","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14731268","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"17185412","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PDB","id":"4KBB","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10932256","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14731268","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4KBB","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 626
ChainResidueDetails
AHIS230metal ligand
AGLN231proton acceptor, proton donor
ATYR234metal ligand
AGLU268metal ligand
AARG370electrostatic stabiliser

site_idMCSA2
Number of Residues
DetailsM-CSA 626
ChainResidueDetails

246031

PDB entries from 2025-12-10

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