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3FFZ

Domain organization in Clostridium butulinum neurotoxin type E is unique: Its implication in faster translocation

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0005576cellular_componentextracellular region
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0008289molecular_functionlipid binding
A0008320molecular_functionprotein transmembrane transporter activity
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0020002cellular_componenthost cell plasma membrane
A0030430cellular_componenthost cell cytoplasm
A0033644cellular_componenthost cell membrane
A0035821biological_processmodulation of process of another organism
A0044161cellular_componenthost cell cytoplasmic vesicle
A0044164cellular_componenthost cell cytosol
A0044221cellular_componenthost cell synapse
A0044231cellular_componenthost cell presynaptic membrane
A0046872molecular_functionmetal ion binding
A0071806biological_processprotein transmembrane transport
A0090729molecular_functiontoxin activity
B0004222molecular_functionmetalloendopeptidase activity
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
B0035821biological_processmodulation of process of another organism
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
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A1300
ChainResidue
AHIS212
AHIS216
AGLU251
AHOH1289
AHOH1318

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A1301
ChainResidue
AHOH1317
AALA544
AGLU547
AGLN548
ALYS550

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A1302
ChainResidue
AVAL593
AILE596
AALA597
AILE599
AHOH1314

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT A1303
ChainResidue
ATYR879
ATYR1041

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B1300
ChainResidue
BHIS212
BHIS216
BGLU251
BHOH1275
BHOH1284

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA B1302
ChainResidue
BVAL593
BILE596
BILE599
BSER600
BHOH1283

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT B1303
ChainResidue
BTYR879
BTYR881

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TLMHELIHSL
ChainResidueDetails
ATHR209-LEU218

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues98
DetailsRegion: {"description":"Belt","evidences":[{"source":"PubMed","id":"19118561","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues444
DetailsRegion: {"description":"N-terminus of receptor binding domain (N-RBD)","evidences":[{"source":"PubMed","id":"19118561","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsMotif: {"description":"Host ganglioside-binding motif","evidences":[{"source":"UniProtKB","id":"P0DPI0","evidenceCode":"ECO:0000250"},{"source":"PubMed","id":"19650874","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15157097","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"},{"source":"PDB","id":"1T3A","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1T3C","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ZKW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ZKX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ZL6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ZN3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FFZ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PDB","id":"1T3A","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1T3C","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ZKW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ZKX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ZL6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ZN3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FFZ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1i1e
ChainResidueDetails
AARG348
AGLU251
ATYR351

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1i1e
ChainResidueDetails
BARG348
BGLU251
BTYR351

238582

PDB entries from 2025-07-09

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